|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1098-1680 |
2.44e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1098 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcqeeeeeilrlhQQKEQSLSSLRERLQKAieeeearmre 1177
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------------AELEAELEELRLELEEL---------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1178 eeSQRLSWLRAQVQsstQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnAAK 1257
Cdd:COG1196 280 --ELELEEAQAEEY---ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--EEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1258 EKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVssLQKKIQEAQQKEEAQLQKCLGQVEHRvhqksyh 1337
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE--LAAQLEELEEAEEALLERLERLEEEL------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1338 vAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQ 1417
Cdd:COG1196 424 -EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1418 EQHKRLEDLRRRHREQERKLQ---DLELDLETRAKDV---KARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1491
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAgavAVLIGVEAAYEAAleaALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1492 QLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPhfEP 1571
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA--GG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1572 DLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVW------HLLSAEGVALRSAKEFLVQQTRSMRRRQTALKA 1645
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAeeeeerELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590
....*....|....*....|....*....|....*
gi 2462523754 1646 AQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKE 1680
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1127-1687 |
4.65e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1127 KQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQE 1206
Cdd:COG1196 211 KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1207 ASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEK-----SEQAALNAAKEKALQQLREQLEGERKEAVATLEK 1281
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEeleelEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1282 EHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkcLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHE 1361
Cdd:COG1196 370 AEAELAEAE-EELEELAEELLEALRAAAELAAQLEELEEA--EEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1362 RRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQ--- 1438
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgav 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1439 DLELDLETRAKDV---KARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILD 1515
Cdd:COG1196 527 AVLIGVEAAYEAAleaALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1516 ELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIE-DLRKSLGTNQTKEVSSSL 1594
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRrELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1595 SQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMR 1674
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|...
gi 2462523754 1675 KNLEKETRHLDEM 1687
Cdd:COG1196 767 RELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1183-1716 |
6.99e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1183 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnaaKEKALQ 1262
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1263 QLREQLEGERKEAvatLEKEHSAELERLcssleAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhVAGYE 1342
Cdd:COG1196 308 EERRRELEERLEE---LEEELAELEEEL-----EELEEELEELEEELEEAEEELEEAEAE---------------LAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1343 HELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKR 1422
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1423 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDvqrqvalksEEATATHQQLEEAQKEhTH 1502
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL---------LEAEADYEGFLEGVKA-AL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1503 LLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLRevtveENNASPHFEPDLHIEDLRKSL 1582
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA-----AKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1583 GTNQTKEVSSSLSQSKEDL-YLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVA 1661
Cdd:COG1196 590 AALARGAIGAAVDLVASDLrEADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1662 KDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1716
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1065-1582 |
8.22e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1065 EWKEAEELGEDSAASLSLQLSLQRRStepvappEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcqEEEE 1144
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1145 EILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAER 1224
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1225 ASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSS 1304
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1305 LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVM--------- 1375
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagava 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1376 -------------------------------AKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLE 1424
Cdd:COG1196 528 vligveaayeaaleaalaaalqnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1425 DLRRRHREQERKLQDLELDLETRAKDVKARLA------LLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQK 1498
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAvtlagrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1499 EHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKhfSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDL 1578
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ--LEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
....
gi 2462523754 1579 RKSL 1582
Cdd:COG1196 766 EREL 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1067-1529 |
2.54e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELGEDSAASLSLQLSLQRRSTEPVAppEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcQEEEEEI 1146
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEE--AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1147 LRLhQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQ-SSTQADEDQIRAEQEASLQKLREELESQQKAERA 1225
Cdd:COG1196 403 EEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1226 SLEQKNRqmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSL 1305
Cdd:COG1196 482 LLEELAE--AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1306 QKKIQEAQQKEEAQLQKC-LGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqVMAKAREQYEA 1384
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR---TLVAARLEAAL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1385 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRhREQERKLQDLELDLETRAKDVKARLALLEVQEET 1464
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL-EELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1465 ARREKQQLLDVQRQVALKSEEAtatHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVD 1529
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREEL---LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1065-1600 |
1.65e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.35 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1065 EWKEAEELGEDSAASLSLQLSLQRRSTEPvappEQLSEAAlKAMEEAVAQVLEQDQRhllESKQEKMQQLREKLCQEEEE 1144
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAA-KAEAEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1145 EILRLHQQKEQSLSSLRERLQKAieeEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAER 1224
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKA---DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1225 ASLEQKNRQMLEQLKEEIEASEKSEQAALNA--AKEKAlQQLREQLEgERKEAVATLEKEHSAELERLCSSLEAKHREVV 1302
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeAKKKA-DEAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1303 sslqKKIQEAQQKEEAQLQKCLGQVEHRvhQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQY 1382
Cdd:PTZ00121 1540 ----KKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1383 EAEERKQRAELLGHLTGELERLQRAHERELETVR---------QEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 1453
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKkaeelkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1454 RLALLEVQEETARREKQQLLDVQRQVALKSEEATaTHQQLEEAQKEHTHLLQSNQQLReiLDELQARKLKLESQVDLLQA 1533
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKA 1770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1534 QSQQLQKHFSLEAEAQKKQHLLR--------------EVTVEENNasphfEPDLHIEDlRKSLGTNQTKEVSSSLSQSKE 1599
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRmevdkkikdifdnfANIIEGGK-----EGNLVIND-SKEMEDSAIKEVADSKNMQLE 1844
|
.
gi 2462523754 1600 D 1600
Cdd:PTZ00121 1845 E 1845
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1015-1715 |
1.30e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1015 QSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEEEPPQGPEGQP-----EWKEAEELGEDSAASLSLQLSLQRR 1089
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaedarKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1090 STEP-VAPPEQLSEAALKAMEEAVAQVL---------EQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSS 1159
Cdd:PTZ00121 1166 AEEArKAEDAKKAEAARKAEEVRKAEELrkaedarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1160 LRERLQKAIEEEEARMREEESQRLSWLRAQvqSSTQADEDQiRAEQEASLQKLREElESQQKAERASLEQKNRQMLEQLK 1239
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELK-KAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1240 EEIEASEKSEQAALNAAKE--KALQQLREQLEGERKEAVATLEKEHSAELE-----RLCSSLEAKHREV--VSSLQKKIQ 1310
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeakKKADAAKKKAEEKkkADEAKKKAE 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1311 EAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVE----GEHERRLDKMKEEHQQ------VMAKARE 1380
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkkAEEAKKAEEAKKKAEEakkadeAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1381 QYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRhrEQERKLQDLELDLETRAKDVKARLALLEV 1460
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1461 QEETARREKQQLLDVQRQVAL-KSEEAtathQQLEEAQKEHThllqsnQQLREILDELQARKLKLESQvdllqaqSQQLQ 1539
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALrKAEEA----KKAEEARIEEV------MKLYEEEKKMKAEEAKKAEE-------AKIKA 1622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1540 KHFSLEAEAQKKQHLLREVTVEENNASphfepdlhiEDLRKSLGTNQTKevssslsqskedlyldslsshnvwhllsaeg 1619
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKA---------EELKKAEEENKIK------------------------------- 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1620 valrsaKEFLVQQTRSMRRRQTALKAAQQHWRHelaSAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA----MRKGH 1695
Cdd:PTZ00121 1663 ------AAEEAKKAEEDKKKAEEAKKAEEDEKK---AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAE 1733
|
730 740
....*....|....*....|
gi 2462523754 1696 NLLKKKEEKLNQLESSLWEE 1715
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDE 1753
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1103-1528 |
7.35e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1103 AALKAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLR---ERLQKAIEEEEARMREEe 1179
Cdd:PRK02224 206 ERLNGLESELAELDEEIER--YEEQREQARETRDEA-----DEVLEEHEERREELETLEaeiEDLRETIAETEREREEL- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1180 SQRLSWLRAQVQ------SSTQADEDQIRAEQEASLQKlREELESQQKAERASLEQKnRQMLEQLKEEIE---------- 1243
Cdd:PRK02224 278 AEEVRDLRERLEeleeerDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEEC-RVAAQAHNEEAEslredaddle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1244 --ASEKSEQAAlnaAKEKALQQLREQLEgERKEAVATLEKE-----------------HSAELERLCSSLEAKHREV--- 1301
Cdd:PRK02224 356 erAEELREEAA---ELESELEEAREAVE-DRREEIEELEEEieelrerfgdapvdlgnAEDFLEELREERDELREREael 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1302 ---VSSLQKKIQEAQQKEEAQlqKC--LGQ-VEHRVH-----QKSYHVAGYEHELSSLlREKRQEVEGEHER-------- 1362
Cdd:PRK02224 432 eatLRTARERVEEAEALLEAG--KCpeCGQpVEGSPHvetieEDRERVEELEAELEDL-EEEVEEVEERLERaedlveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1363 -RLDKMKEEHQQVMAKAREQYE-AEERKQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL 1440
Cdd:PRK02224 509 dRIERLEERREDLEELIAERREtIEEKRERAEELRERAAELE----AEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1441 ELDLEtRAKDVKARLALLEVQEETA-----RREKQQLLDVQRQVALKSE-------EATATHQQLEEAQKEHTHLLQSNQ 1508
Cdd:PRK02224 585 KERIE-SLERIRTLLAAIADAEDEIerlreKREALAELNDERRERLAEKrerkrelEAEFDEARIEEAREDKERAEEYLE 663
|
490 500
....*....|....*....|
gi 2462523754 1509 QLREILDELQARKLKLESQV 1528
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEI 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1204-1521 |
8.56e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.17 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 EQEASLQKLREELESQQKAERASLEQKNRQMLE-----QLKEEIEASEKSEQAALNAAKEKALQQLREQ-----LEGERK 1273
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEerkreLERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1274 EAVAtLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgqveHRVHQKSYHVAGYEHELSSLLREKR 1353
Cdd:pfam17380 368 EEIA-MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ---------RKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1354 QEVEGEHERRLDKMKEEH---QQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHKRLEDLRRRH 1430
Cdd:pfam17380 438 RRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKL---------ELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1431 REQERKLQDLELDLETRAKDVKARLALLEVQEEtarREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsnQQL 1510
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEE---RRKQQEMEERRRIQEQMRKATEERSRLEAMERER-------EMM 578
|
330
....*....|.
gi 2462523754 1511 REILDELQARK 1521
Cdd:pfam17380 579 RQIVESEKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1261-1567 |
1.51e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1261 LQQLREQLEGERKEAVATLE-KEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRvhqksyhva 1339
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL--------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1340 gyEHELSSLlREKRQEVEGEHERRLDKMKEEHQQVMAKARE-QYEAEERKQRAELLGHLTGELERLQrAHERELETVRQE 1418
Cdd:COG1196 266 --EAELEEL-RLELEELELELEEAQAEEYELLAELARLEQDiARLEERRRELEERLEELEEELAELE-EELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1419 QHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQK 1498
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1499 EHTHLLQSNQQLREILDELQARKLK-LESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENNASP 1567
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1118-1719 |
5.16e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1118 QDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQAD 1197
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1198 E-DQIRaEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgeRKEAV 1276
Cdd:TIGR02168 387 KvAQLE-LQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE--RLEEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1277 ATLEKEHSAELERLCSSLEAKHREVVSslQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV----------AGYEHELS 1346
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1347 SLLREKRQEVEGEHE----------------------------------RRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1392
Cdd:TIGR02168 541 AALGGRLQAVVVENLnaakkaiaflkqnelgrvtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1393 LLGH------LTGELERLQRAHEREL----------------------ETVRQEQHKRLEDLRRRHREQERKLQDLEL-- 1442
Cdd:TIGR02168 621 LLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1443 -DLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1517
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1518 QARKLKLESQVDLLQAQSQQLQKHF-SLEAEAQK-KQHLLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVSSSLS 1595
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALdELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1596 QSKEDLYLDSLSShnvwhllsaegvalrSAKEFLVQQTRSMRRRQTAlkaaqqhwRHELASAQEvakdppGIKALEDMRK 1675
Cdd:TIGR02168 861 IEELEELIEELES---------------ELEALLNERASLEEALALL--------RSELEELSE------ELRELESKRS 911
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462523754 1676 NLEKETRHLDEMKSAMRkghNLLKKKEEKLNQLESSLWEEASDE 1719
Cdd:TIGR02168 912 ELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLT 952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1008-1715 |
1.23e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1008 IEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPR--SLATEEEPPQGPEGQPEwkEAEELGEDSAASLSLQLS 1085
Cdd:PTZ00121 1047 IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNraDEATEEAFGKAEEAKKT--ETGKAEEARKAEEAKKKA 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1086 LQRRSTEPVAPPEQLSEAalkamEEAvaQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQ 1165
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKA-----EEA--RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAE 1197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1166 KAIEEEEARMREEESQRLSWLRAqvqsstqadEDQIRAEQEASLQKLREELESQQKAEraslEQKNRQMLEQLKEEIEAS 1245
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKA---------EDAKKAEAVKKAEEAKKDAEEAKKAE----EERNNEEIRKFEEARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1246 EKSEQAALNAAKEKALQQLREQLEGER-KEAVATLEKEHSAELERlcsslEAKHREVVSSLQKKIQEAQQKEEAQLQKCl 1324
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKaDEAKKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKKADAAKKKA- 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1325 gqvehRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERL 1404
Cdd:PTZ00121 1339 -----EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1405 QRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKdvkarlalleVQEETARREKQQLLDVQRQVALKSE 1484
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----------AEEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1485 EATATHQQLEEAQKEHTHLLQSNQQLREIlDElqARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENN 1564
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKA-DE--AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1565 ASPHFEPDLHIEDLRKSLGTNQTKEvsssLSQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALK 1644
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEE----AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1645 AAQQHWRHELASAQEVAK--DPPGIKALEDMRKNlEKETRHLDEMKSA---MRKGHNLLKKKEE---KLNQLESSLWEE 1715
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKaeEENKIKAAEEAKKA-EEDKKKAEEAKKAeedEKKAAEALKKEAEeakKAEELKKKEAEE 1714
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1500 |
1.40e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1146 ILRLHQQKEQSLSSLR------ERLQKAIEEeearmreeesqrlswLRAQVQS-STQADedqiRAEQeasLQKLREELES 1218
Cdd:TIGR02168 167 ISKYKERRKETERKLErtrenlDRLEDILNE---------------LERQLKSlERQAE----KAER---YKELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1219 QQKAERA-SLEQKNRQmLEQLKEEIEASE---KSEQAALNAAKEK------ALQQLREQLEGERKE------AVATLEKE 1282
Cdd:TIGR02168 225 LELALLVlRLEELREE-LEELQEELKEAEeelEELTAELQELEEKleelrlEVSELEEEIEELQKElyalanEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1283 ---HSAELERLCSSLEAKHREVVSSLQKKiqEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehELSSLLREKRQEVEgE 1359
Cdd:TIGR02168 304 kqiLRERLANLERQLEELEAQLEELESKL--DELAEELAELEEKLEELKEELE-----------SLEAELEELEAELE-E 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQD 1439
Cdd:TIGR02168 370 LESRLEELEEQLETL-RSKVAQLELQIASLNNEI-ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462523754 1440 LELDLETRAKDVKARLALLEVQEETARrekQQLLDVQRQVALKSEEATATHQQLEEAQKEH 1500
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1109-1716 |
1.44e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.55 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1109 EEAVAQVLEQDQRHLLESKQEKMQQLREKLCQeeeeeILRLHQQKEQSLSSLRERLQKAieeeeaRMREEESQRLSWLRA 1188
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKH-----LREALQQTQQSHAYLTQKREAQ------EEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1189 QVQSSTQadedqiraeQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALnaakEKALQQLREQL 1268
Cdd:TIGR00618 268 RIEELRA---------QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR----AKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1269 egerkeavatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1348
Cdd:TIGR00618 335 -------------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1349 lrekrqevegeherrLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRR 1428
Cdd:TIGR00618 402 ---------------LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1429 RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQLEEaqkEHTHLLQS 1506
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQ---TYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1507 NQQLREILDELQARKLKLESQVDLLQAQSQQ-LQKHFSLEAEAQKKQHLLREV---TVEENNASPHFEPDLHIEDLRKSL 1582
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1583 GTNQtKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGV--ALRSAKEFlvqQTRSMRRRQTALKAAQQ------HWRHEL 1654
Cdd:TIGR00618 624 EQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVreHALSIRVL---PKELLASRQLALQKMQSekeqltYWKEML 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523754 1655 ASAQEvakdppgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEA 1716
Cdd:TIGR00618 700 AQCQT---------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQA 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1067-1712 |
3.23e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELGEDSAASLSLQLSLQRRSTEpvappEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEI 1146
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLD-----ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1147 LRLHQ---QKEQSLSSLRERLQKAieeeeARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAE 1223
Cdd:TIGR02168 382 ETLRSkvaQLELQIASLNNEIERL-----EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1224 RASLEQKN--RQMLEQLKEEIEASEKSEQAAlnAAKEKALQQLREQLEGERKEAVATLEKEH--SAELERLCSSLEAKHR 1299
Cdd:TIGR02168 457 ERLEEALEelREELEEAEQALDAAERELAQL--QARLDSLERLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1300 -----EVV--SSLQ----KKIQEAQQKEEAQLQKCLGQVehrvhqksyhvagyehELSSLLREKRQEVEGEHERRLdkMK 1368
Cdd:TIGR02168 535 yeaaiEAAlgGRLQavvvENLNAAKKAIAFLKQNELGRV----------------TFLPLDSIKGTEIQGNDREIL--KN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1369 EEHQQVMAKAREQYEAEERKQRAELLGH------LTGELERLQRAHEREL----------------------ETVRQEQH 1420
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1421 KRLEDLRRRHREQERKLQDLEL---DLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEATATHQQL 1493
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQLSKEL 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1494 EEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHF-SLEAEAQK-KQHLLREVTVEENNASPHFEP 1571
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdELRAELTLlNEEAANLRERLESLERRIAAT 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1572 DLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHL-----LSAEGVALRSAKEFLVQQTRSMRRRQTALKAA 1646
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerasLEEALALLRSELEELSEELRELESKRSELRRE 916
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462523754 1647 QQHWRHELASAQEVakdppgIKALEDMRKNL-----EKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1712
Cdd:TIGR02168 917 LEELREKLAQLELR------LEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1109-1520 |
5.01e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1109 EEAVAQVLEQDQRHL-LESKQEKMQQLREKLcQEEEEEILRLHQQKEQSLSSLRERLQkaieeeearmreEESQRLSWLR 1187
Cdd:TIGR02168 666 AKTNSSILERRREIEeLEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELE------------ELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1188 AQVQSSTQadEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKEkALQQLREQ 1267
Cdd:TIGR02168 733 KDLARLEA--EVEQLEERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKE-ELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1268 LEGERKEavATLEKEHSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAQLQkclgqvehrvhqksyhVAGYEHELSS 1347
Cdd:TIGR02168 805 LDELRAE--LTLLNEEAANLRERLESLERRIAATERRLE---DLEEQIEELSED----------------IESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1348 lLREKRQEVEGEHErRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAHERELETVRQEQHK---RLE 1424
Cdd:TIGR02168 864 -LEELIEELESELE-ALLNERASLEEALALLRSELEELSEELR---------ELESKRSELRRELEELREKLAQlelRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1425 DLR-RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRqVALKS-EEATATHQQLEEAQKEHTH 1502
Cdd:TIGR02168 933 GLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP-VNLAAiEEYEELKERYDFLTAQKED 1011
|
410
....*....|....*...
gi 2462523754 1503 LLQSNQQLREILDELQAR 1520
Cdd:TIGR02168 1012 LTEAKETLEEAIEEIDRE 1029
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1601 |
9.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1106 KAMEEAVAQVLEQDQRhlLESKQEKMQQLREKLcqeeeeEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSW 1185
Cdd:COG4913 221 PDTFEAADALVEHFDD--LERAHEALEDAREQI------ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1186 LRAQVqsstqadeDQIRAEQEAsLQKLREELESQQKAERASLEQKNRQM-------LEQLKEEIEASEKSEQAALNAAK- 1257
Cdd:COG4913 293 LEAEL--------EELRAELAR-LEAELERLEARLDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRRAr 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1258 -EKALQQLREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAqQKEEAQLQKCLGQVEHRVHQKSY 1336
Cdd:COG4913 364 lEALLAALGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDL-RRELRELEAEIASLERRKSNIPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1337 HVAGYEHELSSLLREKRQE---------------------------------VEGEHERR----LDKMKEEHQQVMAKAR 1379
Cdd:COG4913 441 RLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalrwVNRLHLRGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1380 EQYEAEERKQRAEllGHLTGELE------------RLQR-------AHERELET----------VRQEQHKRLEDLRRRH 1430
Cdd:COG4913 521 TGLPDPERPRLDP--DSLAGKLDfkphpfrawleaELGRrfdyvcvDSPEELRRhpraitragqVKGNGTRHEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1431 REQ-------ERKLQDLELD---LETRAKDVKARLALLEVQEETARREKQQLLDVQrQVALKSEEATATHQQLEEAQKEH 1500
Cdd:COG4913 599 RSRyvlgfdnRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1501 THLLQSN---QQLREILDELQARKLKLESQVDllqaqsQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFEPDLHI-- 1575
Cdd:COG4913 678 ERLDASSddlAALEEQLEELEAELEELEEELD------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAll 751
|
570 580
....*....|....*....|....*..
gi 2462523754 1576 -EDLRKSLGTNQTKEVSSSLSQSKEDL 1601
Cdd:COG4913 752 eERFAAALGDAVERELRENLEERIDAL 778
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1000-1517 |
1.92e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.69 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1000 RQAQQPLGIEDKDDSQSSQDELQSKQSKGLEErlsppLPHEERAQSPPRSLATEEEPPQGPEGQpewKEAEELGEDSAAS 1079
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTT-----LTQKLQSLCKELDILQREQATIDTRTS---AFRDLQGQLAHAK 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1080 LSLQLSLQRRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSL-S 1158
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK--KAVVLARLLELQEEPCPLcG 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1159 SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEaSLQKLREELESQQKAERASLEQKNR--QMLE 1236
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRskEDIP 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1237 QLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA---- 1312
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsi 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1313 -QQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSsLLREkrqevEGEHERRLDKMKEEHQQVMAKAREQYEAEE--- 1386
Cdd:TIGR00618 668 rVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQT-LLRE-----LETHIEEYDREFNEIENASSSLGSDLAAREdal 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1387 -------RKQRAELLGHLTGELERLQRAHERELETVRQEQHKRlEDLRRRHREQERKLQDLELDLETRAKDVKARLALLE 1459
Cdd:TIGR00618 742 nqslkelMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN 820
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1460 VQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL 1517
Cdd:TIGR00618 821 LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1098-1719 |
1.98e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.70 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1098 EQLSEAALKAMEEAVAQVLEQDQRHLLEsKQEKMQQLREKLCQ--EEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARM 1175
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELK-LQELKLKEQAKKALeyYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1176 REEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM------LEQLKEEIEASEKSE 1249
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrkvdDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1250 QAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkCLGQVEH 1329
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-LKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1330 RVHQKSYHVAGYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghltgELERLQRAHE 1409
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLKDELEL-------KKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1410 RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALkSEEATAT 1489
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV-IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1490 HQQLEEAQKEHTHLLQSNQQLREIldELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEEnNASPHF 1569
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKL--RLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG-ILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1570 EPDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSshnvwhLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQH 1649
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL------TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1650 WRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEEASDE 1719
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1067-1475 |
2.81e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELGEDSAASLSLQLSLQRRSTEpvappeQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLcQEEEEEI 1146
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEE------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1147 LRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSW---LRAQVQSSTQADEDQIRAEQEASLQKLREELEsQQKAE 1223
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLK-AAKAG 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1224 RASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERkEAVATLEKEHSAELERLCSSLEAKHREVvS 1303
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREV-T 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1304 SLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSyhvagyehELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE 1383
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELE--------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1384 AEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEV 1460
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLAIEEYEELEERYDFLSE 802
|
410
....*....|....*
gi 2462523754 1461 QEETARREKQQLLDV 1475
Cdd:COG1196 803 QREDLEEARETLEEA 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1102-1475 |
5.11e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRERLQKAieeeearmreeeSQ 1181
Cdd:TIGR02168 683 EEKIEELEEKIAEL--EKALAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQL------------EE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1182 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREElesqqkAERASLEQKNRQMLEQLKEEIEASeKSEQAALNAAKEKAl 1261
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1262 QQLREQLEGERKEAVATlekehSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQlqkclgQVEHRVHQKSYHVAGY 1341
Cdd:TIGR02168 820 ANLRERLESLERRIAAT-----ERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1342 EHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKareQYEAEERKQRAELLghLTGELERLQRAHERELETVRQEQHK 1421
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVR--IDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1422 RLED---LRRRHREQERKLQDL---ELDLETRAKDVKARLALLEVQEETARREKQQLLDV 1475
Cdd:TIGR02168 963 IEDDeeeARRRLKRLENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1124-1557 |
6.78e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1124 LESKQEKMQQLREKLcqeeeeeilRLHQQKEQSLSSLRERLQKAieeeeARMREEESQRLSWLRAQVQsstQADEDQIRA 1203
Cdd:COG4717 73 LKELEEELKEAEEKE---------EEYAELQEELEELEEELEEL-----EAELEELREELEKLEKLLQ---LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 EQEASLQKLREELES--QQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEKALQQLREQLEgERKEAVATLEK 1281
Cdd:COG4717 136 ALEAELAELPERLEEleERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELE-ELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1282 EhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQV------EHRVHQKSYHVAGYEHELSSLLREKRQE 1355
Cdd:COG4717 214 E-LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1356 VEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER 1435
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1436 KlqdlELDLETRAKDVKARLALLEvQEETARREKQQLLDVQRQVA--LKSEEATATHQQLEEAQKEHTHLLQSNQQLREI 1513
Cdd:COG4717 373 A----ALLAEAGVEDEEELRAALE-QAEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462523754 1514 LDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLRE 1557
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1102-1517 |
7.33e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE-EILRLHQQKEQSLSSLRERLQkaieeeearmreEE 1179
Cdd:COG4717 77 EEELKEAEEKEEEYAElQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELA------------EL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1180 SQRLSWLRAQVQSSTQADEDQIRAEQEasLQKLREELESQQKAERASLEQKNRQMLEQLkEEIEASEKSEQAALNAAKEK 1259
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1260 aLQQLREQLEGERKEAVATLEKEHSAELERL-------------------------------------CSSLEAKHREVV 1302
Cdd:COG4717 222 -LEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1303 SSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA- 1378
Cdd:COG4717 301 GKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAg 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1379 ----------------REQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1442
Cdd:COG4717 381 vedeeelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523754 1443 DLETRAKDvkARLALLEVQEETARREKQQLldVQRQVALKseeatATHQQLEEAQKEHTHLLQS--NQQLREILDEL 1517
Cdd:COG4717 461 ELEQLEED--GELAELLQELEELKAELREL--AEEWAALK-----LALELLEEAREEYREERLPpvLERASEYFSRL 528
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1219-1527 |
5.82e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.10 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1219 QQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEgerkeavatlEKEHSAELERLcssLEAKH 1298
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE----------EREQKRQEEYE---EKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1299 REVVSSLQKKIQEAQQKEEAQLQKclgqvehRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKA 1378
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLE-------KQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1379 REQYEAEERKQR-AELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDlETRAKDVKARLAL 1457
Cdd:pfam13868 173 AEREEIEEEKEReIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ-QAREEQIELKERR 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1458 LEVQEETARREKQQLLDVQR-QVALKSEEATATHQQLEEAQKEHTHLLQSNQQLR--EILDELQARKLKLESQ 1527
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRaaEREEELEEGERLREEE 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1453 |
1.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 EQEASLQKLREELESQQKAERASLEQKNRQMLEqLKEEIEA------------SEKSEQAALNAAKEKALQQLREQLEGE 1271
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEElqkelyalaneiSRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1272 R----------KEAVATLEKEhSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAqLQKCLGQVEHRVHQKSYHVAGY 1341
Cdd:TIGR02168 325 LeeleskldelAEELAELEEK-LEELKEELESLEAELEE----LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1342 EHELSSLlrEKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHK 1421
Cdd:TIGR02168 399 NNEIERL--EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270
....*....|....*....|....*....|....
gi 2462523754 1422 RLEDLRRRHREQERK--LQDLELDLETRAKDVKA 1453
Cdd:TIGR02168 477 LDAAERELAQLQARLdsLERLQENLEGFSEGVKA 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1192-1709 |
1.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1192 SSTQADEDQIRAEQEASLQKLRE--ELESQQKAERASLE--QKNRQMLEQLKEEIEASEKSEQAALNAAK--EKALQQLR 1265
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREinEISSELPELREELEklEKEVKELEELKEEIEELEKELESLEGSKRklEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1266 EQLEGERKE-------------------AVATLEKEHSAELERL--CSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQK 1322
Cdd:PRK03918 266 ERIEELKKEieeleekvkelkelkekaeEYIKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEErlEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1323 CLGQVEHRVHQKSYHVAGYEhELSSLLREKRQEVEGEHERRLDKMKEEHQQVmAKAREQYEAEERKQRAELlGHLTGELE 1402
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEEL-EKAKEEIEEEISKITARI-GELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1403 RLQRAHErELETVRQ---------EQHKRLEDLRRRHREQERKLQDLElDLETRAKDVKARLALLEVQeetarREKQQLL 1473
Cdd:PRK03918 423 ELKKAIE-ELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKV-----LKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1474 DVQRQVA--LKSEEATATHQQLEEAQKEHTHLlqsnQQLREILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKK 1551
Cdd:PRK03918 496 IKLKELAeqLKELEEKLKKYNLEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELE-------------KLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1552 QHLLREV-TVEENNASphfepdlhIEDLRKSLGTNQTKEVSSSLsQSKEDLYLDSLSSHNVWHLLSAEGVALRSAKEFLV 1630
Cdd:PRK03918 559 AELEKKLdELEEELAE--------LLKELEELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1631 Q----------QTRSMRRRQTALKAAQQHWRHE------LASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKG 1694
Cdd:PRK03918 630 KafeelaetekRLEELRKELEELEKKYSEEEYEelreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
570
....*....|....*
gi 2462523754 1695 HNLLKKKEEKLNQLE 1709
Cdd:PRK03918 710 KKELEKLEKALERVE 724
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1146-1716 |
1.76e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.53 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1146 ILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERA 1225
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1226 SLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQlreQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSL 1305
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK---KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1306 QKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE-A 1384
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELElK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1385 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1464
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1465 ARREKQQLLDvqrqvaLKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSL 1544
Cdd:pfam02463 481 KLQEQLELLL------SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1545 EAEAQKKQHLLREVTVEENNAsphfepdlhieDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVALRS 1624
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPL-----------GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1625 AKEFLVQQTRSMRRRQTALKAAQ--QHWRHELASAQEVAKDPPGIKALEDMRKN--LEKETRHLDEMKSAMRKGHNLLKK 1700
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESglRKGVSLEEGLAEKSEVKASLSELTKELLEiqELQEKAESELAKEEILRRQLEIKK 703
|
570
....*....|....*.
gi 2462523754 1701 KEEKLNQLESSLWEEA 1716
Cdd:pfam02463 704 KEQREKEELKKLKLEA 719
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1113-1455 |
2.47e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 64.17 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1113 AQVLEQDQRHLLESKQEK-----MQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLR 1187
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERrldemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1188 AQVQssTQADEDQIRAEQEASLQKLREELEsQQKAERASLEQKNRQMLEQL----------KEEIEASEKSEQAALNAAK 1257
Cdd:pfam13868 106 IVER--IQEEDQAEAEEKLEKQRQLREEID-EFNEEQAEWKELEKEEEREEderileylkeKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1258 EKALQQLREQLEGERKeavatlEKEHSAEL--ERLCSSLEAKHRevvsslQKKIQEAQQKEEAQLQKCLGQVEHRVHqks 1335
Cdd:pfam13868 183 EREIARLRAQQEKAQD------EKAERDELraKLYQEEQERKER------QKEREEAEKKARQRQELQQAREEQIEL--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1336 yhvagyehelssllREKRQEVEGEHERRLDKMKEEHQQVMAKaREQYEAEERKQRaellghltgelerlQRAHERELETV 1415
Cdd:pfam13868 248 --------------KERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMK--------------RLEHRRELEKQ 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462523754 1416 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1455
Cdd:pfam13868 299 IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1085-1474 |
2.65e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1085 SLQRRSTEPVAPPEQLSEAALKAMEEAVaqvleQDQRHLLESKQEKMQQLREKLCQEeeeeiLRLHQQKEQSLSSLRERL 1164
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGL-----KRELSSLQSELRRIENRLDELSQE-----LSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1165 QKaieeeearMREEESQRLSWLRAQVQSSTQADEDQIR---------AEQEASLQKLREELESQQKAERASLEQKNRQML 1235
Cdd:TIGR02169 729 EQ--------EEEKLKERLEELEEDLSSLEQEIENVKSelkeleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1236 EQLKEEIeaSEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEkehsaelerlcssleakhrevvsSLQKKIQEAQQK 1315
Cdd:TIGR02169 801 SKLEEEV--SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI-----------------------DLKEQIKSIEKE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1316 EEAqLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRqevegEHERRLDKMKEEHQQvmAKAREQYEAEERKQRAELLG 1395
Cdd:TIGR02169 856 IEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEE--LEAQIEKKRKRLSELKAKLE 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1396 HLTGELERLQRAHERELETVRQEQhkRLEDLRRRHREQERKLQDLElDLETRA----KDVKARLALLEVQEETARREKQQ 1471
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALE-PVNMLAiqeyEEVLKRLDELKEKRAKLEEERKA 1004
|
...
gi 2462523754 1472 LLD 1474
Cdd:TIGR02169 1005 ILE 1007
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1071-1485 |
9.20e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1071 ELGEDSAASLSLQLSLQRRSTEPVAPPEQLSEAALkameEAVAQVLEQDQRHLLESKQekMQQLREKLcqeeeeeilrlh 1150
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQ--FEKIAEEL------------ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1151 QQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIR-AEQEASLQKLR-EELESQQKAERASLE 1228
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnIELTAHCDKLLlENKELTQEASDMTLE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1229 QKNRQ------------MLEQLkEEIEASEKSEQAALNAAKEKALQQ-------LREQLEGERKEAVATLEKEHSAE-LE 1288
Cdd:pfam05483 515 LKKHQediinckkqeerMLKQI-ENLEEKEMNLRDELESVREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKiLE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1289 RLCSSLeakhREVVSSLQKKIQEAQQKEEAQLQKC------LGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGE--- 1359
Cdd:pfam05483 594 NKCNNL----KKQIENKNKNIEELHQENKALKKKGsaenkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkis 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRLDKMKEEHQQVMAKAREQYEAEERKQraellgHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQerklQD 1439
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQ------HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ----SS 739
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462523754 1440 LELDLETRAKDVKARLALLEVQEETARREKQQL-LDVQRQVALKSEE 1485
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLkMEAKENTAILKDK 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1187-1528 |
1.71e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.43 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1187 RAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERAsLE---QKNRQMLEQLKEEIEASEKSE--QAALNAAKEKAL 1261
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESD-LEqdyQAASDHLNLVQTALRQQEKIEryQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1262 QQ--LREQLEGERKEAVATLEkEHSAELERLCSSLeAKHREVVSSLQKKIQEAQQKEEAqlqkcLGQVEHRVHQKSYHVA 1339
Cdd:COG3096 365 EQeeVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL-ADYQQALDVQQTRAIQYQQAVQA-----LEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1340 GYEHELSSLlREKRQEVegeHERRLDKmkEEHQQVMAKAREQYEaeerkQRAELLGHLTGELERLQrAHE--RE-LETVR 1416
Cdd:COG3096 438 NAEDYLAAF-RAKEQQA---TEEVLEL--EQKLSVADAARRQFE-----KAYELVCKIAGEVERSQ-AWQtaRElLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1417 QEQH--KRLEDLRRRHREQERKL---QDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1491
Cdd:COG3096 506 SQQAlaQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1492 QLEE-----------------AQKEHTHL-------LQSNQQLREIL--------------DELQARKLKLESQV 1528
Cdd:COG3096 586 QLEQlrarikelaarapawlaAQDALERLreqsgeaLADSQEVTAAMqqllerereatverDELAARKQALESQI 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1185-1499 |
2.08e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1185 WLRAQVQSSTQADEDQIRAeQEASLQKLREELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALnaaKEKALQQL 1264
Cdd:TIGR02169 226 YELLKEKEALERQKEAIER-QLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRV---KEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1265 REQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAgyehE 1344
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRAELE----E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1345 LSSLLREKRQEVEgEHERRLDKMKEEHQQVMakaREQYEAEERKQRAEL-LGHLTGELERLQRAHeRELETvrqeqhkRL 1423
Cdd:TIGR02169 376 VDKEFAETRDELK-DYREKLEKLKREINELK---RELDRLQEELQRLSEeLADLNAAIAGIEAKI-NELEE-------EK 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1424 EDLRRRHREQERKLQDLELDLEtrakdvKARLALLEVQEETARREKQqlldvQRQVALKSEEATATHQQLEEAQKE 1499
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLS------KYEQELYDLKEEYDRVEKE-----LSKLQRELAEAEAQARASEERVRG 508
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1186-1578 |
2.43e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1186 LRAQVQSStqadEDQIRAEQEAsLQKLREELEsQQKAERASLEQKNRQMLEQLKEEIEA---SEKSEQAalnaakEKALQ 1262
Cdd:PRK04863 291 LRRELYTS----RRQLAAEQYR-LVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTAlrqQEKIERY------QADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1263 QLREQLEgERKEAVAtLEKEHSAELERLCSSLEakhrEVVSSLQKKIQEAQQKEEAQlQKCLGQVEHRVH-----QKSYH 1337
Cdd:PRK04863 359 ELEERLE-EQNEVVE-EADEQQEENEARAEAAE----EEVDELKSQLADYQQALDVQ-QTRAIQYQQAVQaleraKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1338 VAGYEHE-LSSLLREKRQEVEGEHERRLDKmkeEHQQVMAK-AREQYEaeerkQRAELLGHLTGELERlQRAHERELETV 1415
Cdd:PRK04863 432 LPDLTADnAEDWLEEFQAKEQEATEELLSL---EQKLSVAQaAHSQFE-----QAYQLVRKIAGEVSR-SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1416 RQ-EQHK----RLEDLRRRHREQERKLQdLELDLETRAKDVKARLAL-----LEVQEETARREkQQLLDVQRQVALKSEE 1485
Cdd:PRK04863 503 RRlREQRhlaeQLQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddeDELEQLQEELE-ARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1486 ATATHQQLEEAQKEHTHLLQSNQQLREildeLQARKLKLESQVDLLQAQsqqlqkhfSLEAEAQKKQHLLREVTVEENN- 1564
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQSGEEFED--------SQDVTEYMQQLLERERELTVERd 648
|
410
....*....|....*.
gi 2462523754 1565 --ASPHFEPDLHIEDL 1578
Cdd:PRK04863 649 elAARKQALDEEIERL 664
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1102-1717 |
2.77e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVLEQ--DQRHLLESKQEKMQQLREKLCQEEEEEILRLhQQKEQSLSSLRERLQKAIEEEEarmreee 1179
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKE------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1180 sQRLSWLRAQVQsstQADEDqiRAEQEASLQKLREELESQQKaERASLE---QKNRQMLEQLKEEIEASEKSEQAA---L 1253
Cdd:TIGR02169 315 -RELEDAEERLA---KLEAE--IDKLLAEIEELEREIEEERK-RRDKLTeeyAELKEELEDLRAELEEVDKEFAETrdeL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1254 NAAKEK--ALQQLREQLEGERKEAVATLEKEHS--AELERLCSSLEAKHREVVS---SLQKKIQEAQQKEEaQLQKCLGQ 1326
Cdd:TIGR02169 388 KDYREKleKLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1327 VEHRVHQKSYHVAGYEHELSSLLRE-------KRQEVEGEHERR-------------------LDKMKEEHQ---QVMAK 1377
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRElaeaeaqARASEERVRGGRaveevlkasiqgvhgtvaqLGSVGERYAtaiEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1378 AREQY---EAEERKQRA-ELL-----GHLTGELERLQRAHERELETVRQ-----------EQHKRLE------------- 1424
Cdd:TIGR02169 547 NRLNNvvvEDDAVAKEAiELLkrrkaGRATFLPLNKMRDERRDLSILSEdgvigfavdlvEFDPKYEpafkyvfgdtlvv 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1425 ---DLRRRHREQERkLQDLELDL-----------------ETRAKDVKARLALLEVQEETARREKQQLLD----VQRQVA 1480
Cdd:TIGR02169 627 ediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSelrrIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1481 LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkhfsLEAEAQKKQHLLREVTV 1560
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE----------------IENVKSELKELEARIEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1561 EENNASphfEPDLHIEDLRKSLGTNQTKEVSSSLSQSKE-----DLYLDSL-SSHNVWHLLSAegvALRSAKEFLVQQTR 1634
Cdd:TIGR02169 770 LEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEevsriEARLREIeQKLNRLTLEKE---YLEKEIQELQEQRI 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1635 SMRRRQTALKAAQQHWRHELAS-AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLW 1713
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEElEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
....
gi 2462523754 1714 EEAS 1717
Cdd:TIGR02169 924 AKLE 927
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1067-1715 |
3.49e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 62.30 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELGEDSAASLSLQLSLQRRSTEPVAPPEQLSEAALKAMEEAVAQ----VLEQDQRHLLESKQEKMQQLREKLCQEE 1142
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1143 EEEILRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKA 1222
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1223 ERAS--LEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLRE------QLEGERKEAVATLEKEHSAELERLCSSL 1294
Cdd:pfam02463 412 ELARqlEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQElkllkdELELKKSEDLLKETQLVKLQEQLELLLS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1295 EAKHREVVSSLQKKIQEAQQKEEAQLQK---CLGQVEHRVHQKSYHVAGYEHELSSLL-----REKRQEVEGEHERR--- 1363
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVivevsATADEVEERQKLVRalt 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1364 ------------LDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERE-LETVRQEQHKRLEDLRRRH 1430
Cdd:pfam02463 572 elplgarklrllIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDtELTKLKESAKAKESGLRKG 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1431 REQERKLQDLELDLETRAKDVKARLALLEVQEetARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQL 1510
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQE--KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1511 REILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLG-TNQTKE 1589
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEE 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1590 VSSSLSQSKEDLYLDSLSSH---NVWHLLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPPG 1666
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKikeEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462523754 1667 IKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEE 1715
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1223-1719 |
3.76e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1223 ERAS--------LEQKNRQMLEQLKEEIEASEKSE-QAALNAAkEKALQQLREQL---EGERKEAVATLEK------EHS 1284
Cdd:PRK02224 169 ERASdarlgverVLSDQRGSLDQLKAQIEEKEEKDlHERLNGL-ESELAELDEEIeryEEQREQARETRDEadevleEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1285 AELERLcSSLEAKHREvvssLQKKIQEAQQKEEAqlqkclgqVEHRVHQKSYHVAGYEHELSSLLREkrQEVEGEHERRL 1364
Cdd:PRK02224 248 ERREEL-ETLEAEIED----LRETIAETEREREE--------LAEEVRDLRERLEELEEERDDLLAE--AGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1365 DKMKEEHQQVMAKAREQYEaEERKQRAELLGHLTGELERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLEL 1442
Cdd:PRK02224 313 EARREELEDRDEELRDRLE-ECRVAAQAHNEEAESLREDADDLEERaeELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1443 DLEtrakDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS------NQQL------ 1510
Cdd:PRK02224 392 EIE----ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVegsphv 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1511 ------REILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHllREVTVEEnnasphfepdlHIEDLRKSLgt 1584
Cdd:PRK02224 468 etieedRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE--RREDLEE-----------LIAERRETI-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1585 NQTKEVSSSLSQSKEDlyldslsshnvwhlLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDP 1664
Cdd:PRK02224 533 EEKRERAEELRERAAE--------------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1665 PGIKALEDMRKNLEKETRHLDEMKSAMRKghnLLKKKEEKLNQLESSLWEEASDE 1719
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRE---RLAEKRERKRELEAEFDEARIEE 650
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1105-1723 |
1.02e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.83 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1105 LKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLCQEEEE----------EILRLHQQKEQSLSSLRERLQKAIEEEEA 1173
Cdd:TIGR00606 254 LKEIEHNLSKIMKlDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlnDLYHNHQRTVREKERELVDCQRELEKLNK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1174 RMREEESQRLSWLRAQVQSSTQAD--EDQIRAEQEASLQ-KLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQ 1250
Cdd:TIGR00606 334 ERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSlATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1251 AALNAAKEKALQQLREQLEGERKEAVATLEKEhSAELERLCSSLeakhREVVSSLQK---------KIQEAQQKEEAQLQ 1321
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL----KFVIKELQQlegssdrilELDQELRKAERELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1322 KClgQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHErrLDKMKEEHQQVMAKAREQYEAEER------KQRAELLG 1395
Cdd:TIGR00606 489 KA--EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQirkiksRHSDELTS 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1396 HL-----TGELERLQRAHERELETVR------QEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARlallEVQEET 1464
Cdd:TIGR00606 565 LLgyfpnKKQLEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS----QDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1465 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVdllqaqSQQLQKHFSL 1544
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL------RLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1545 EAEAQKKQHLLREVTVE-ENNASPHFEPDLHIEDLRkslgtNQTKEVSSSLSQSKEDLYLDSlsshnvwHLLSAEGVALR 1623
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLaPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQE-------TLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1624 SAKEFLVQQTrSMRRRQTALKAAQQHWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEE 1703
Cdd:TIGR00606 783 SAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
650 660
....*....|....*....|
gi 2462523754 1704 KLNQLESSLWEEASDEGTLG 1723
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIG 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1000-1528 |
1.93e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1000 RQAQQPLGIEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQspprslateEEPPQGPEGQPEWKEAEELGEDSAAS 1079
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---------ERINRARKAAPLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1080 LSLQLSLQRRSTEPVAPPEQLSEAALKAMEEAVAQVLEQD---QRHLLESKQEKMQQLREKLCQEEEEE--ILRLHQQKE 1154
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQQHTLTqhIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1155 ------QSLSSLRERLQK---------------AIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLR 1213
Cdd:TIGR00618 390 tltqklQSLCKELDILQReqatidtrtsafrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1214 EELE--------SQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKE-KALQQLREQLEGERK---EAVATLEK 1281
Cdd:TIGR00618 470 EREQqlqtkeqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQRGEQTYAqleTSEEDVYH 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1282 EHSAELERLcSSLEAKHREVVSSLQKKIQEAQQ-KEEAQ-LQKCLGQVEHRVHQKSyhvagyEHELSSLLREKRQEVEGE 1359
Cdd:TIGR00618 550 QLTSERKQR-ASLKEQMQEIQQSFSILTQCDNRsKEDIPnLQNITVRLQDLTEKLS------EAEDMLACEQHALLRKLQ 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRL--------DKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQR--AHERELE---------------- 1413
Cdd:TIGR00618 623 PEQDLqdvrlhlqQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrqLALQKMQsekeqltywkemlaqc 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1414 -TVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKdvkarlALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQ 1492
Cdd:TIGR00618 703 qTLLRELETHIEEYDREFNEIENASSSLGSDLAARED------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT 776
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462523754 1493 LEEAQkehtHLLQSNQQLREILDELQARKLKLESQV 1528
Cdd:TIGR00618 777 GAELS----HLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1488 |
2.10e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1250 QAALNAAKEKALQQLREQLEgERKEAVATLEKEHSAELERLcssleAKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEH 1329
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-----AALERRIAALARRIRALEQ-ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1330 RVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRahe 1409
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1410 rELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1488
Cdd:COG4942 168 -ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1182-1527 |
2.28e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1182 RLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL---ESQQKAERASLEQKN---------RQMLEQLKEEIEASEKSE 1249
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADevleeheerREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1250 qaalnAAKEKALQQLREQLEgERKEAVATLEKEHSAELERlcSSLEAKHREVVSSLqkkiQEAQQKEEAQLQKCLGQVEH 1329
Cdd:PRK02224 268 -----AETEREREELAEEVR-DLRERLEELEEERDDLLAE--AGLDDADAEAVEAR----REELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1330 RVHQKSYHVAGYEHELSSL------LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-----KQRAELLGHLT 1398
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLeeraeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1399 GELERLQRAHER--ELETVRQEQHKRLEDLRR------------------------RHREQERKLQDLELDLETRAKDVK 1452
Cdd:PRK02224 416 ELREERDELREReaELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1453 ARLALLEVQEETARR---EKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREildelQARKLKLESQ 1527
Cdd:PRK02224 496 ERLERAEDLVEAEDRierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE-----AAAEAEEEAE 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1272-1565 |
3.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1272 RKEAVATLEKEhSAELERLcsslEAKHREVVSSLQKKIQEAQQKEEAQ-LQKCLGQVEHRVHQKSYHVAGYE-HELSSLL 1349
Cdd:TIGR02168 174 RKETERKLERT-RENLDRL----EDILNELERQLKSLERQAEKAERYKeLKAELRELELALLVLRLEELREElEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 REKRQEVEgEHERRLDKMKEEHQQVMAkarEQYEAEERKQRA-ELLGHLTGELERL------QRAHERELETVRQEQHKR 1422
Cdd:TIGR02168 249 KEAEEELE-ELTAELQELEEKLEELRL---EVSELEEEIEELqKELYALANEISRLeqqkqiLRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1423 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQV-ALKSEEATATHQ---------- 1491
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLeTLRSKVAQLELQiaslnneier 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1492 ---QLEEAQKEHTHLLQSNQQLREILDElqARKLKLESQVDLLQAQSQQLQKHF-SLEAEAQKKQHLLREVTVEENNA 1565
Cdd:TIGR02168 405 leaRLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELeRLEEALEELREELEEAEQALDAA 480
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1118-1529 |
3.51e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1118 QDQRHLLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlraqVQSSTQAD 1197
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMAREL-----AELNEAESDLEQDYQAASDHLNL-----------------------VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1198 EDQIRAEqeASLQKLREELESQQKAERASLEQK--NRQMLEQLKEEIEaSEKSE----QAALNAAKEKALQQlreqlege 1271
Cdd:PRK04863 348 EKIERYQ--ADLEELEERLEEQNEVVEEADEQQeeNEARAEAAEEEVD-ELKSQladyQQALDVQQTRAIQY-------- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1272 rKEAVATLEKehsaeLERLC--SSLEAKhrevvsSLQKKIQEAQQKEEAQLQKCLgQVEHRVHQKSYHVAGYEHELSSLL 1349
Cdd:PRK04863 417 -QQAVQALER-----AKQLCglPDLTAD------NAEDWLEEFQAKEQEATEELL-SLEQKLSVAQAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 RekrqeVEGEHERrldkmKEEHQQVMAKAREqyeAEERKQRAELLGHLTGELERLQRAH--ERELETVRQEQHKRL---- 1423
Cdd:PRK04863 484 K-----IAGEVSR-----SEAWDVARELLRR---LREQRHLAEQLQQLRMRLSELEQRLrqQQRAERLLAEFCKRLgknl 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1424 ---EDLRRRHREQERKLQDLELDLET-RAKDVKARLALLEVQEETARREKQQLLDVQRQVAL-----KSEEATATHQQLE 1494
Cdd:PRK04863 551 ddeDELEQLQEELEARLESLSESVSEaRERRMALRQQLEQLQARIQRLAARAPAWLAAQDALarlreQSGEEFEDSQDVT 630
|
410 420 430
....*....|....*....|....*....|....*
gi 2462523754 1495 EAQKEHTHLLQSNQQLReilDELQARKLKLESQVD 1529
Cdd:PRK04863 631 EYMQQLLERERELTVER---DELAARKQALDEEIE 662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1086-1520 |
3.62e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1086 LQRRSTEPVAppEQLSE--AALKAMEEAVAQVLEQdQRHL--LESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLR 1161
Cdd:COG4913 218 LEEPDTFEAA--DALVEhfDDLERAHEALEDAREQ-IELLepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1162 ERLQKaieeeearmreeesqrlswLRAQVQSsTQADEDQIRAEQEASLQKLREelesqqkAERASLEQKNRQmLEQLKEE 1241
Cdd:COG4913 295 AELEE-------------------LRAELAR-LEAELERLEARLDALREELDE-------LEAQIRGNGGDR-LEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1242 IEASEKSEQAALNAAK--EKALQQLREQLEGERkEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQqKEEAQ 1319
Cdd:COG4913 347 IERLERELEERERRRArlEALLAALGLPLPASA-EEFAALRAEAAALLEAL-EEELEALEEALAEAEAALRDLR-RELRE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1320 LQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKRQE---------------------------------VEGEHERR--- 1363
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllVPPEHYAAalr 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1364 -LDKMKEEHQQVMAKAREQYEAEERKQ-----------------RAELLGHL-----------TGELERLQRA------- 1407
Cdd:COG4913 504 wVNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqv 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1408 ------HE----------------------------RELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 1453
Cdd:COG4913 584 kgngtrHEkddrrrirsryvlgfdnraklaaleaelAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV 663
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523754 1454 RLALLEVQEetARREKQQLLD-------VQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1520
Cdd:COG4913 664 ASAEREIAE--LEAELERLDAssddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1203-1462 |
3.83e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1203 AEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKaLQQLREQLEGERKEaVATLEK 1281
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE-YEKLKEKLIKLKGE-IKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1282 EHS--AELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEAQLQKCLGQVEhRVHQKSYHVAGYEHELSSLLREKRQEv 1356
Cdd:PRK03918 547 ELEklEELKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKL- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1357 egehERRLDKMKEEHQQVMAKARE----------QYEAEERKQRAELLGHLTGELERLqRAHERELETVRQEQHKRLEDL 1426
Cdd:PRK03918 625 ----EEELDKAFEELAETEKRLEElrkeleelekKYSEEEYEELREEYLELSRELAGL-RAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462523754 1427 RRRHREQERKLQDLEL---------DLETRAKDVKARL---ALLEVQE 1462
Cdd:PRK03918 700 KEELEEREKAKKELEKlekalerveELREKVKKYKALLkerALSKVGE 747
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1360-1549 |
4.35e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQEQHKRLEDLRRRHREQERKLQD 1439
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1440 LEldleTRAKDVKARLALLEVQEETARREKQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1518
Cdd:COG4717 144 LP----ERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|.
gi 2462523754 1519 ARKLKLESQVDLLQAQSQQLQKHFSLEAEAQ 1549
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1206-1440 |
5.27e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.43 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1206 EASLQKLRE---ELESQQKAERASlEQKNRQMLEQLKEEIEASEK-SEQAALNAAKEKA--LQQLREQLEgERKEAVATL 1279
Cdd:COG3096 835 EAELAALRQrrsELERELAQHRAQ-EQQLRQQLDQLKEQLQLLNKlLPQANLLADETLAdrLEELREELD-AAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1280 EK--EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSLLRE 1351
Cdd:COG3096 913 QQhgKALAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIfaLSEVVQRRPHFSYEDAvgllGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1352 KRQEVEGEHERRLDKMK------EEHQQVMAKAREQYEAeerkqRAELLGHLTGELERL---------QRAHER------ 1410
Cdd:COG3096 992 RLEQAEEARREAREQLRqaqaqySQYNQVLASLKSSRDA-----KQQTLQELEQELEELgvqadaeaeERARIRrdelhe 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462523754 1411 ----------ELETVRQEQHKRLEDLRRRHREQERKLQDL 1440
Cdd:COG3096 1067 elsqnrsrrsQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-1724 |
5.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1408 HERELETVR-----QEQHKRLEDLRRrhrEQERKLQDLEL---------DLETRAKDVKARLALLEVQEETARRE--KQQ 1471
Cdd:TIGR02168 171 KERRKETERklertRENLDRLEDILN---ELERQLKSLERqaekaerykELKAELRELELALLVLRLEELREELEelQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1472 LLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQQLQKHFS-----LEA 1546
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1547 EAQKKQHLLREVT-VEENNASphFEPDlhIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDslsshnvwhlLSAEGVALRS 1624
Cdd:TIGR02168 328 LESKLDELAEELAeLEEKLEE--LKEE--LESLEAELEElEAELEELESRLEELEEQLET----------LRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1625 AKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPpgikALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEK 1704
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|
gi 2462523754 1705 LNQLESSLWEEASDEGTLGG 1724
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1340-1687 |
6.31e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1340 GYEHELSSLLREKRqEVEGEHERRLDKMKEEHQQV--MAKAREQYEAEERKQRAELlghltGELERLQRAHERELETVRQ 1417
Cdd:TIGR02169 685 GLKRELSSLQSELR-RIENRLDELSQELSDASRKIgeIEKEIEQLEQEEEKLKERL-----EELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1418 EqhkrLEDLRRRHREQERKLQDLELDLEtrakDVKARLALLEVQEETARREKqqlldVQRQVALKSEEATATHQQLEEAQ 1497
Cdd:TIGR02169 759 E----LKELEARIEELEEDLHKLEEALN----DLEARLSHSRIPEIQAELSK-----LEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1498 KEHTHLLQSNQQLREILDELQARKLKLESQVDLLQAQSQqlqkhfSLEAEAQKKQHLLREVTVEennasphfepdlhIED 1577
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE------ELEEELEELEAALRDLESR-------------LGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1578 LRKslgtnQTKEVSSSLSQSKEdlyldslsshnvwhllsaegvALRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASA 1657
Cdd:TIGR02169 887 LKK-----ERDELEAQLRELER---------------------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
330 340 350
....*....|....*....|....*....|
gi 2462523754 1658 QEVAKDPPGIKALEDMRKNLEKETRHLDEM 1687
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1115-1485 |
6.33e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1115 VLEQDQRHLLESKQEKMQQLREKLcQEEEEEILRLHQQKEQsLSSLRERLQKAIEEEEARMREEESQR-LSWLRAQVQSS 1193
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEEL-AEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEReIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1194 TQADED-----QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASekseQAALNAAKEKALQQLREQL 1268
Cdd:COG4913 681 DASSDDlaaleEQLEELEAELEELEEELD-ELKGEIGRLEKE----LEQAEEELDEL----QDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1269 EGERKEA-VATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvEHRVHQKSYHvaGYEHELSS 1347
Cdd:COG4913 752 EERFAAAlGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA------DLDADLESLP--EYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1348 LLREKRQEVEGEHERRLDKMKEEH----QQVMAKAREqyEAEERkqraelLGHLTGELERLQRAHERELE-TVRQEQHKR 1422
Cdd:COG4913 824 LEEDGLPEYEERFKELLNENSIEFvadlLSKLRRAIR--EIKER------IDPLNDSLKRIPFGPGRYLRlEARPRPDPE 895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1423 LEDLRRRHREQERKLQDLELDL-ETRAKDVKARLALLEVQE-ETARREKQQLLDVQRQVALKSEE 1485
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELsEARFAALKRLIERLRSEEeESDRRWRARVLDVRNHLEFDAEE 960
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1124-1715 |
6.62e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1124 LESKQEKMQQLREKLCQeeeeeilrLHQQKEQSLSSLRERLQKAIEEEEARMReeesqrlswLRAQVQSSTQADEDQIRA 1203
Cdd:pfam15921 115 LQTKLQEMQMERDAMAD--------IRRRESQSQEDLRNQLQNTVHELEAAKC---------LKEDMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 ---EQEASLQKLR------EELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLrEQLEGERKE 1274
Cdd:pfam15921 178 mmlSHEGVLQEIRsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1275 AVATLEKEHSAELERLCSSLE----------AKHREVVSSLQKK---IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagy 1341
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQleiIQEQARNQNSMYMRQLSDLESTVSQ-------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1342 eheLSSLLREKRQEVEgeherrlDKMKEEHQQVMAKAREQYEAE-ERKQRAELLGHLTGELERL-QRAHERELE-TVRQE 1418
Cdd:pfam15921 329 ---LRSELREAKRMYE-------DKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLlADLHKREKElSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1419 QHKRLED-----------LRRRHREQERKLQDLELDLETRAKDVKARL---------------------ALLEVQEETAR 1466
Cdd:pfam15921 399 QNKRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMerqmaaiqgkneslekvssltAQLESTKEMLR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1467 REKQQLldVQRQVALKSEEAT-----ATHQQLEEA------------------QKEHTHLLQSNQQLREILDELQARKLK 1523
Cdd:pfam15921 479 KVVEEL--TAKKMTLESSERTvsdltASLQEKERAieatnaeitklrsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1524 ----------LESQVDLLQA--------QSQQLQKHFSLEAEAQKKQHLLREVTVEENNASPHFE------PDLHIEDLR 1579
Cdd:pfam15921 557 maekdkvieiLRQQIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelearvSDLELEKVK 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1580 KSLGTNQTKEVSSSLSQSKEDLYLDSLSSHNVWHLLSAEGVAL----RSAKEFLVQQTRSMRRRQTALKAAQQHWRHELA 1655
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1656 SAQevAKDPPGIKALEDMRKNLEKETRHLDEMKSAMR----------KGHNLLKKKEEKLNQLESSLWEE 1715
Cdd:pfam15921 717 SME--GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtnanKEKHFLKEEKNKLSQELSTVATE 784
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1070-1529 |
8.32e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1070 EELGEDSAASLSLQLslqrrstEPVAppeqlSEAALKAMEEAVAQVLEQDQRHLLESKQekmqqLREKLCQEEEEeiLRL 1149
Cdd:pfam01576 110 EQLDEEEAARQKLQL-------EKVT-----TEAKIKKLEEDILLLEDQNSKLSKERKL-----LEERISEFTSN--LAE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1150 HQQKEQSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADE--DQIR------AEQEASLQKLREELES--- 1218
Cdd:pfam01576 171 EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDlqEQIAelqaqiAELRAQLAKKEEELQAala 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1219 ---QQKAERASLEQKNRQMLEQLKEEIEASEkSEQAALNAAkEKALQQLREQLEGERKEAVATL-----EKEHSAELERL 1290
Cdd:pfam01576 251 rleEETAQKNNALKKIRELEAQISELQEDLE-SERAARNKA-EKQRRDLGEELEALKTELEDTLdttaaQQELRSKREQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1291 CSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKS---YHVAGYEHELSSLLREKR--QEVEGEHERRLD 1365
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAnleKAKQALESENAELQAELRtlQQAKQDSEHKRK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1366 KMKEEHQQVMAKAREQyeAEERKQRAELLGHLTGELERLQRAHErELETVRQEQHKRLEDLrrrhreqERKLQDLE--LD 1443
Cdd:pfam01576 409 KLEGQLQELQARLSES--ERQRAELAEKLSKLQSELESVSSLLN-EAEGKNIKLSKDVSSL-------ESQLQDTQelLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1444 LETRAK------------DVKARLALLEVQEETARREKQQLLDVQRQVA---LKSEEATATHQQLEEAQKEHTHLLQS-N 1507
Cdd:pfam01576 479 EETRQKlnlstrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmkKKLEEDAGTLEALEEGKKRLQRELEAlT 558
|
490 500
....*....|....*....|....*
gi 2462523754 1508 QQLRE---ILDELQARKLKLESQVD 1529
Cdd:pfam01576 559 QQLEEkaaAYDKLEKTKNRLQQELD 583
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1105-1483 |
8.62e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 57.27 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1105 LKAMEEAVAQVLEQDQrhllESKQEKMQQLREKlcqeeeeeILRLHQQKEQ---SLSSLRERLQKAIeeeearmreeesQ 1181
Cdd:COG5185 248 LAQTSDKLEKLVEQNT----DLRLEKLGENAES--------SKRLNENANNlikQFENTKEKIAEYT------------K 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1182 RLSWLRAQVQSSTQADedqiRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE----------EIEASEKSEQA 1251
Cdd:COG5185 304 SIDIKKATESLEEQLA----AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAikeeienivgEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1252 -----ALNAAKEKALQQLREQlEGERKEAVATLE---KEHSAELERLCSSLEAKHREVvsslqkkiqEAQQKEEAQLQKC 1323
Cdd:COG5185 380 dsfkdTIESTKESLDEIPQNQ-RGYAQEILATLEdtlKAADRQIEELQRQIEQATSSN---------EEVSKLLNELISE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1324 LGQVEHRVhqksyhvagyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREqyeaeerkqraellghLTGELER 1403
Cdd:COG5185 450 LNKVMREA----------DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST----------------LKATLEK 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1404 LQRAHERELETVRQEQHKRLEDLRRRHREQErklQDLELDLETRAKDVKARLALLE--VQEETARREKQQLLDVQRQVAL 1481
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELIQASNAktDGQAANLRTAVIDELTQYLSTI 580
|
..
gi 2462523754 1482 KS 1483
Cdd:COG5185 581 ES 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1183-1418 |
9.00e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1183 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrqmLEQLKEEIEASEK------SEQAALNA- 1255
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARriraleQELAALEAe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1256 -----AKEKALQQLREQLEGERKEAVATLEKEHSA-ELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEH 1329
Cdd:COG4942 85 laeleKEIAELRAELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1330 RVHQKSYHVAgyehELSSLLREKRQEvegehERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHE 1409
Cdd:COG4942 165 LRAELEAERA----ELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLE 233
|
....*....
gi 2462523754 1410 RELETVRQE 1418
Cdd:COG4942 234 AEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1305-1711 |
9.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1305 LQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL-----LREKRQEVEgEHERRLDKMKEEHQQVMAK 1377
Cdd:COG4717 76 LEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLekllqLLPLYQELE-ALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1378 AREQYEAEERKQRAEllghltGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAKDVKAR 1454
Cdd:COG4717 155 LEELRELEEELEELE------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaqeELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1455 LALLEVQEETArREKQQLLDVQRQVALKSE--EATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR-KLKLESQVDll 1531
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAReKASLGKEAE-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1532 qaqsqqlqkhfslEAEAQKKQHLLREVTVEENNASPHFEPDLHIEDLRKSLGT-NQTKEVSSSLSQSKEDLYLDSLSSHN 1610
Cdd:COG4717 306 -------------ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1611 VwHLLSAEGVALRSAKEFLVQQTrsmrRRQTALKAAQQHWRHELASAQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSA 1690
Cdd:COG4717 373 A-ALLAEAGVEDEEELRAALEQA----EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420
....*....|....*....|.
gi 2462523754 1691 MRKGHNLLKKKEEKLNQLESS 1711
Cdd:COG4717 448 LEELREELAELEAELEQLEED 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1347-1712 |
1.03e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1347 SLLREKRQEVEgeheRRLDKMKEEHQQVMAKARE---QYEAEERK-QRAELLGHLTGELERLQRA--------HERELET 1414
Cdd:TIGR02168 168 SKYKERRKETE----RKLERTRENLDRLEDILNElerQLKSLERQaEKAERYKELKAELRELELAllvlrleeLREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1415 VRQEqhkrLEDLRRRHREQERKLQDLELDLETrakdvkARLALLEVQEETARREK------QQLLDVQRQVALKSEEATA 1488
Cdd:TIGR02168 244 LQEE----LKEAEEELEELTAELQELEEKLEE------LRLEVSELEEEIEELQKelyalaNEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1489 THQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKKQHLLREVTveennasph 1568
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------------SLEAELEELEAELEELE--------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1569 fepdLHIEDLRKSLGTnqtkeVSSSLSQSKEDLYLdslsshnvwhlLSAEGVALRSAKEFLVQQTRSMRRRQTALKAAQQ 1648
Cdd:TIGR02168 372 ----SRLEELEEQLET-----LRSKVAQLELQIAS-----------LNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523754 1649 HWRHELASAQEVAKDppgiKALEDMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1712
Cdd:TIGR02168 432 EAELKELQAELEELE----EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1300-1715 |
1.50e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1300 EVVSSLQKKIQEAQQ--KEEAQLQKCLGQVEHRVHQKSYHVagyeHELSSLLREKRQEVEGEHER--RLDKMKEEhqqvM 1375
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEvkELEELKEE----I 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1376 AKAREQYEAEERKQRA--ELLGHLTGELERLqRAHERELETVRQE---------QHKRLEDLRRRHREQERKLQDLELDL 1444
Cdd:PRK03918 241 EELEKELESLEGSKRKleEKIRELEERIEEL-KKEIEELEEKVKElkelkekaeEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1445 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQV------ALKSEEATATHQQLEEAQKEHTHLlqSNQQLREILDELQ 1518
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1519 ARKLKLESQVDLLQAQSQqlqkhfSLEAEAQKKQHLLREVTvEENNASPHFEPDLHiEDLRKSLGTNQTKEVSSSLSQSK 1598
Cdd:PRK03918 398 KAKEEIEEEISKITARIG------ELKKEIKELKKAIEELK-KAKGKCPVCGRELT-EEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1599 EdlyLDSLSSHnvwhlLSAEGVALRSakeFLVQQTRSMRRRQTA--LKAAQQHWR-HELASAQEVAKDPPGIK----ALE 1671
Cdd:PRK03918 470 E---IEEKERK-----LRKELRELEK---VLKKESELIKLKELAeqLKELEEKLKkYNLEELEKKAEEYEKLKekliKLK 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462523754 1672 DMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSLWEE 1715
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1100-1288 |
1.79e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1100 LSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKlcqeeeeeILRLHQQKEQSLSSLRERLQkaieeeearmreee 1179
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--------IHKLRNEFEKELRERRNELQ-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1180 sqrlswlraQVQSSTQADEDQIRAEQEaSLQKLREELESQQKaeraSLEQKNRQmLEQLKEEIEASEKSEQAAL----NA 1255
Cdd:PRK12704 86 ---------KLEKRLLQKEENLDRKLE-LLEKREEELEKKEK----ELEQKQQE-LEKKEEELEELIEEQLQELerisGL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 2462523754 1256 AKEKALQQLREQLEGE-RKEAVATL-EKEHSAELE 1288
Cdd:PRK12704 151 TAEEAKEILLEKVEEEaRHEAAVLIkEIEEEAKEE 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1186-1325 |
1.97e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 53.92 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1186 LRAQVQSSTQADED------QIRAEQEASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE- 1258
Cdd:pfam04012 9 VRANIHEGLDKAEDpekmleQAIRDMQSELVKARQALA-QTIARQKQLERR----LEQQTEQAKKLEEKAQAALTKGNEe 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1259 ---KALQQlREQLEG--ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQK-KIQEAQQKEEAQLQKCLG 1325
Cdd:pfam04012 84 larEALAE-KKSLEKqaEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlKARLKAAKAQEAVQTSLG 155
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1203-1392 |
3.21e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1203 AEQEASLQKLREELESQQKAERASLEQKnrQMLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEgERKEAvatLEKE 1282
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEK-ELRERRNELQKLEKRLLQKEENLD-RKLEL---LEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1283 hSAELERLCSSLEAKHREvvssLQKKIQEAQQKEEAQLQKCLgqvehrvhqksyHVAGYEHElssllrEKRQEVegeher 1362
Cdd:PRK12704 109 -EEELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELE------------RISGLTAE------EAKEIL------ 159
|
170 180 190
....*....|....*....|....*....|
gi 2462523754 1363 rLDKMKEEHQQVMAKAREQYEaEERKQRAE 1392
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIE-EEAKEEAD 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1116-1528 |
4.03e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1116 LEQDQRHLLESKQEKMQQLREKlcqeeEEEILRLHQQKEQSLSSL---RERLQKAIEEEEARmreeeSQRLSWLRAQVQS 1192
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEK-----TTEISNTQTQLNQLKDEQnkiKKQLSEKQKELEQN-----NKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1193 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQ--KNRQMLEQLKEEIEASEKSEQAalnaaKEKALQQLREQLEg 1270
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTN-----SESENSEKQRELE- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1271 ERKEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVAGYEHELSSL 1348
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEqiKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1349 lREKRQEVEGEHERrLDKMKEEHQQVMAKAREQYEAEER--KQRAELLGHLTGELERLQRaHERELE------TVRQEQH 1420
Cdd:TIGR04523 446 -TNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNE-EKKELEekvkdlTKKISSL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1421 K-RLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQE---------------ETARREKQQLL--------DVQ 1476
Cdd:TIGR04523 523 KeKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknkeieelkqtqkslKKKQEEKQELIdqkekekkDLI 602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462523754 1477 RQVALKSEEATATHQQLEEAQKEhthllqsNQQLREILDELQARKLKLESQV 1528
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKE-------NEKLSSIIKNIKSKKNKLKQEV 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1120-1328 |
5.05e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1120 QRHLLESKQEKMQQLREKLcqEEEEEILRLHQQKEQSLSSLRERLQKAIEeEEARMREEESQRLSWLRAQVQsSTQADED 1199
Cdd:COG4942 18 QADAAAEAEAELEQLQQEI--AELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAALEAELA-ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1200 QIRAEQEASLQKLREELESQQKAERASLEQ------------KNRQMLEQLKEEIEaseksEQAALNAAKEKALQQLREQ 1267
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARR-----EQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523754 1268 LEGERKEaVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQ------QKEEAQLQKCLGQVE 1328
Cdd:COG4942 169 LEAERAE-LEALLAELEEERAAL-EALKAERQKLLARLEKELAELAaelaelQQEAEELEALIARLE 233
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1038-1458 |
5.54e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.91 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1038 PHEERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSLQLSLQRRSTepvaPPEQLSEAALKAMEEAVAQVLE 1117
Cdd:PLN02939 38 RRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKST----SSDDDHNRASMQRDEAIAAIDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1118 QDQRHLLESKQEKMQQLRE--KLCQEEEEEILRLHQQKEQSLSSL------RERLQKAIEEEEarmreeesQRLSWLRAQ 1189
Cdd:PLN02939 114 EQQTNSKDGEQLSDFQLEDlvGMIQNAEKNILLLNQARLQALEDLekilteKEALQGKINILE--------MRLSETDAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1190 VQSSTQadeDQIRAE-QEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEieasekseqaalNAAKEKALQQLREQL 1268
Cdd:PLN02939 186 IKLAAQ---EKIHVEiLEEQLEKLRNELLIRGATEGLCVHSLSKE-LDVLKEE------------NMLLKDDIQFLKAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1269 E--GERKEAVATLEKEHSAeLERLCSSLEAK---HREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQksyhvagyeh 1343
Cdd:PLN02939 250 IevAETEERVFKLEKERSL-LDASLRELESKfivAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEK---------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1344 elSSLLREKRQEVegehERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGhltgelERLQRAHERELETVR--QEQHK 1421
Cdd:PLN02939 319 --AALVLDQNQDL----RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLE------ERLQASDHEIHSYIQlyQESIK 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462523754 1422 RLEDLRRRHREQERKlQDLELDLETRAKDVKARLALL 1458
Cdd:PLN02939 387 EFQDTLSKLKEESKK-RSLEHPADDMPSEFWSRILLL 422
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1098-1513 |
7.55e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.14 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1098 EQLSEAALKAMEEAVAQVLEQD-----QRHLLESKQEKMQQLREKLCQ-EEEEEILRLHQQKEQSLSSLRERLQKAIEEE 1171
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGleaalALVRSGEGKALMDEIRARLLLlALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1172 EARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA 1251
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1252 ALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQVEHRV 1331
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA----ALALLA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1332 HQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERE 1411
Cdd:COG5278 349 ALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEAL 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1412 LETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQ 1491
Cdd:COG5278 429 AEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAAL 508
|
410 420
....*....|....*....|..
gi 2462523754 1492 QLEEAQKEHTHLLQSNQQLREI 1513
Cdd:COG5278 509 LLAAAEAALAAALAAALASAEL 530
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1234-1524 |
7.59e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.50 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1234 MLEQLKEEIEASEKSEQAALNAAKEK-ALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEA 1312
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRrRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1313 QQKEEAQLQKclgqVEHRVHQKsyhvagyehelsslLREKRQEVEG---EHERRLdKMKEEHQQVMaKAREQYEAEERKQ 1389
Cdd:pfam15558 93 ESRWREQAED----QENQRQEK--------------LERARQEAEQrkqCQEQRL-KEKEEELQAL-REQNSLQLQERLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1390 RAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLqDLELDLeTRAKDVKARLALLEVQE--ETARR 1467
Cdd:pfam15558 153 EACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRL-SLEQSL-QRSQENYEQLVEERHRElrEKAQK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1468 EKQQLLDVQRqVALKSEEATATHQQL------EEAQKEHTHLLQSNQQLREILDELQARKLKL 1524
Cdd:pfam15558 231 EEEQFQRAKW-RAEEKEEERQEHKEAlaeladRKIQQARQVAHKTVQDKAQRARELNLEREKN 292
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1105-1475 |
8.99e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1105 LKAMEEAVAQ------VLEQDQRHLLESKQEKMQQLREKLCQ-----EEEEEILRLHQQKEQSLSSLRERLQKAIEEEEA 1173
Cdd:pfam12128 310 LSAADAAVAKdrseleALEDQHGAFLDADIETAAADQEQLPSwqselENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1174 RMREEESQRLSWLR-------AQVQSSTQADEDQIRAEQEASLQKLREE-LESQQKAERASLEQKNRQMLEQLKEEIEAS 1245
Cdd:pfam12128 390 RDIAGIKDKLAKIReardrqlAVAEDDLQALESELREQLEAGKLEFNEEeYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1246 E------KSEQAALNAAKEkALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHreVVSSLQKKIQEAQQKEEAQ 1319
Cdd:pfam12128 470 DerieraREEQEAANAEVE-RLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL--QLFPQAGTLLHFLRKEAPD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1320 LQKCLGQVE-----HRVHQKSYHVAGYEHELSSL----LREKRQEV------EGEHERRLDKMKEEHQQVMAKAREQYEA 1384
Cdd:pfam12128 547 WEQSIGKVIspellHRTDLDPEVWDGSVGGELNLygvkLDLKRIDVpewaasEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1385 eerkqraelLGHLTGELERLQRAHERELETV--------------RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKD 1450
Cdd:pfam12128 627 ---------LVQANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKK 697
|
410 420
....*....|....*....|....*
gi 2462523754 1451 VKARLALLEVQEETARREKQQLLDV 1475
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQV 722
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1003-1316 |
1.02e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 53.99 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1003 QQPLGIEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRSLATEEEPPQGPEGQPEWKEAEELGEDSAASLSL 1082
Cdd:pfam09731 57 LAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1083 QLSLQRRSTEPVAPPE----QLSEAALKAMEEAVAQVLEQDQ------RHLLESKQEKMQQLREKLCQEEEEEILRLHQQ 1152
Cdd:pfam09731 137 AISKAESATAVAKEAKddaiQAVKAHTDSLKEASDTAEISREkatdsaLQKAEALAEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1153 KEQSLSSLRERLQKAIEEEEArmreeeSQRLSWLRAQVQSSTqADEDQIRAEQEAS------------------------ 1208
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEK------AQSLAKLVDQYKELV-ASERIVFQQELVSifpdiipvlkednllsnddlnsli 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1209 ------LQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKE 1282
Cdd:pfam09731 290 ahahreIDQLSKKLAELKKREEKHIERA----LEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK 365
|
330 340 350
....*....|....*....|....*....|....
gi 2462523754 1283 HSAELERLCSSLEAKHREVVSSLQKKIQEAQQKE 1316
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQD 399
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1215-1558 |
1.17e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1215 ELESQQKAERASLEQKNRQMlEQLKEEIEASEKSEQAALNAAK---------EKALQQLREQLEGERKEA---------- 1275
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKaleedlqiaTKTICQLTEEKEAQMEELnkakaahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1276 -------VATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQK---------EEAQLQKCLGQVEHRVHQK----- 1334
Cdd:pfam05483 351 vtefeatTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMtkfknnkevELEELKKILAEDEKLLDEKkqfek 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1335 -SYHVAGYEHELSSLLREKRQEVEG-EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGH---LTGELERL-QRAH 1408
Cdd:pfam05483 430 iAEELKGKEQELIFLLQAREKEIHDlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkLLLENKELtQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1409 ERELETVRQEQH------------KRLEDLRRRHREQERKLQDLELDLETRAKDVKARLallEVQEETARREKQQLLDVQ 1476
Cdd:pfam05483 510 DMTLELKKHQEDiinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL---DKSEENARSIEYEVLKKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1477 RQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREI-------LDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQ 1549
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgsaenkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
410
....*....|.
gi 2462523754 1550 K--KQHLLREV 1558
Cdd:pfam05483 667 KisEEKLLEEV 677
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1203-1453 |
1.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1203 AEQEASLQKLREELeSQQKAERASLEQKNRQM---LEQLKEEIEASEKSE-QAAL--NAAKEKALQQLREQLEgERKEAV 1276
Cdd:PRK04863 833 ADPEAELRQLNRRR-VELERALADHESQEQQQrsqLEQAKEGLSALNRLLpRLNLlaDETLADRVEEIREQLD-EAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1277 ATLEK--EHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKC--LGQVEHRVHQKSYHVA----GYEHELSSL 1348
Cdd:PRK04863 911 RFVQQhgNALAQLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAfaLTEVVQRRAHFSYEDAaemlAKNSDLNEK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1349 LREKRQEVEGEherrLDKMKEEHQQ----------VMAKAREQYEA-----EERKQRAELLG-HLTGELERLQRAHEREL 1412
Cdd:PRK04863 990 LRQRLEQAEQE----RTRAREQLRQaqaqlaqynqVLASLKSSYDAkrqmlQELKQELQDLGvPADSGAEERARARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462523754 1413 etvrqeqHKRLEDLRRRHREQERKLQDLELDLETRAKDVKA 1453
Cdd:PRK04863 1066 -------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1188-1386 |
1.29e-06 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 53.33 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1188 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERasleQKNRQMLEQLKEEIEASEKSEQAALNaaKEKALQQLREQ 1267
Cdd:PRK00106 62 AKRESKALKKELLLEAKEEA--RKYREEIEQEFKSER----QELKQIESRLTERATSLDRKDENLSS--KEKTLESKEQS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1268 LE------GERKEAVATLEKEHSAELERLCSSLEAKHREVVsslqkkiqeaqqkeeaqlqkcLGQVEHRVhqksyhvagy 1341
Cdd:PRK00106 134 LTdkskhiDEREEQVEKLEEQKKAELERVAALSQAEAREII---------------------LAETENKL---------- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462523754 1342 EHELSSLLREKRQEVegehERRLDKM-KEEHQQVMAKAREQYEAEE 1386
Cdd:PRK00106 183 THEIATRIREAEREV----KDRSDKMaKDLLAQAMQRLAGEYVTEQ 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1338-1516 |
1.52e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1338 VAGYEHELSSLLREKRQEVEGEHERRLDKMKEEhqqvMAKAREQYEAEERKQRAELlghltGELERLQRAHERELEtvrq 1417
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE----IHKLRNEFEKELRERRNEL-----QKLEKRLLQKEENLD---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1418 eqhKRLEDLRRRhreqERKLQDLELDLETRAKDVKARlallevQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQ 1497
Cdd:PRK12704 100 ---RKLELLEKR----EEELEKKEKELEQKQQELEKK------EEELEELIEEQLQELERISGLTAEEAKE--ILLEKVE 164
|
170
....*....|....*....
gi 2462523754 1498 KEHTHllQSNQQLREILDE 1516
Cdd:PRK12704 165 EEARH--EAAVLIKEIEEE 181
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1361-1526 |
1.54e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1361 ERRLDKMKEEHQQVMAKAREqyEAEERKQRAELlghltgelerlqrahereleTVRQEQHKRLEDLRRRHREQERKLQDL 1440
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIKKEALL--------------------EAKEEIHKLRNEFEKELRERRNELQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1441 EldletraKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHthllqsNQQLREI--LDELQ 1518
Cdd:PRK12704 88 E-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ------LQELERIsgLTAEE 154
|
....*...
gi 2462523754 1519 ARKLKLES 1526
Cdd:PRK12704 155 AKEILLEK 162
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1188-1319 |
1.93e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1188 AQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1267
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQER--QKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1268 LEGERK-------EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQ 1319
Cdd:TIGR02794 128 QAAEAKakaeaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAE 186
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1204-1437 |
2.38e-06 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 50.43 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 EQEASLQKLREelesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAAlnaakeKALQQLREQLEGERKEAVATLEK-E 1282
Cdd:pfam15665 11 EHEAEIQALKE----AHEEEIQQILAETREKILQYKSKIGEELDLKRRI------QTLEESLEQHERMKRQALTEFEQyK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1283 HSAELERLCssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvehrvhqksyhvagyehelsslLREKRQEVEGEHER 1362
Cdd:pfam15665 81 RRVEERELK--AEAEHRQRVVELSREVEEAKRAFEEKLES--------------------------FEQLQAQFEQEKRK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1363 RLDKMKEEHQQVMAKAREQYEAEERKqraellghLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKL 1437
Cdd:pfam15665 133 ALEELRAKHRQEIQELLTTQRAQSAS--------SLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKL 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1386-1665 |
2.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1386 ERKQRAELLGHLTGELERLQRAHErELETVRqEQHKRLEDLRRRHREQERKLQDLEL--DLETRAKDVKA--RLALLEVQ 1461
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHE-ALEDAR-EQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAqrRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1462 EETARREKQQLldvQRQVALKSEEATATHQQLEEAQKEHthLLQSNQQLREILDELQARKLKLESQvdllqaqsqqlqkh 1541
Cdd:COG4913 297 LEELRAELARL---EAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEER-------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1542 fslEAEAQKKQHLLREVtveennaspHFEPDLHIEDLRKSLgtNQTKEVSSSLSQSKEDLyldslssHNVWHLLSAEGVA 1621
Cdd:COG4913 358 ---ERRRARLEALLAAL---------GLPLPASAEEFAALR--AEAAALLEALEEELEAL-------EEALAEAEAALRD 416
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462523754 1622 LRSAKEFLVQQTRSMRRRQTALKAAQQHWRHELASAQEVAKDPP 1665
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1102-1520 |
3.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEeeeilRLHQQKEQSLSSLRERLQKAIEEEEARMREEESQ 1181
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-----RELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1182 RLSW--LRAQVQSSTQADEDQiRAEQEASLQKLREELEsQQKAERASLEQKN-------RQMLEQLKEEIEASE------ 1246
Cdd:COG4913 386 RAEAaaLLEALEEELEALEEA-LAEAEAALRDLRRELR-ELEAEIASLERRKsniparlLALRDALAEALGLDEaelpfv 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1247 ------KSEQAALNAAKEKAL-----------------------QQLREQLEGERKEAVATLEKEHSAELERLCSSLEAK 1297
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaltllvppehyaaalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFK 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1298 ----HREVVSSLQKKIQEAQQKEEAQLQKC------LGQV--EHRVHQK-------SYHVAGYE-----HELSSLLREKR 1353
Cdd:COG4913 544 phpfRAWLEAELGRRFDYVCVDSPEELRRHpraitrAGQVkgNGTRHEKddrrrirSRYVLGFDnraklAALEAELAELE 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1354 QEVEgEHERRLDKMKEEHQQvMAKAREQYEAEERKQRAEL--------LGHLTGELERLQRAHE--RELETVRQEQHKRL 1423
Cdd:COG4913 624 EELA-EAEERLEALEAELDA-LQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDdlAALEEQLEELEAEL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1424 EDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQ-KEHTH 1502
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIdALRAR 781
|
490
....*....|....*...
gi 2462523754 1503 LLQSNQQLREILDELQAR 1520
Cdd:COG4913 782 LNRAEEELERAMRAFNRE 799
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1201-1558 |
3.41e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1201 IRAEQEASLQKLREELESQQkaerASLEQKNRQMLEQLKEEIEASEksEQAALNAAKEKALQQLREQLEGERKEavatlE 1280
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKELEEELKEAE--EKEEEYAELQEELEELEEELEELEAE-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1281 KEHSAELERLcssleakhrEVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQksyhVAGYEHELSSlLREKRQEVEG 1358
Cdd:COG4717 112 EELREELEKL---------EKLLQLLPLYQELEALEAelAELPERLEELEERLEE----LRELEEELEE-LEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1359 EHERRLDKMKEEHQQVMAKAREQYEA--EERKQRAELLGHLTGELERLQRAHER-ELETVRQEQHKRLEDLRR------- 1428
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLllliaaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1429 -----------------------------------------RHREQERKLQDLELDLETRAKDVKARLALLEVQEETARR 1467
Cdd:COG4717 258 llallglggsllsliltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1468 EKQQLLDVQRQVALKSEEATATHQQL--EEAQKEHTHLLQSNQ-----QLREILD------ELQARKLKLESQVDLLQAQ 1534
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGvedeeELRAALEqaeeyqELKEELEELEEQLEELLGE 417
|
410 420
....*....|....*....|....
gi 2462523754 1535 SQQLQKHFSLEAEAQKKQHLLREV 1558
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEEL 441
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1350-1522 |
4.00e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 1429
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1430 HREQERKLQD-LELDLETR---AKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHT---- 1501
Cdd:pfam13868 111 QEEDQAEAEEkLEKQRQLReeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlr 190
|
170 180
....*....|....*....|.
gi 2462523754 1502 HLLQSNQQLREILDELQARKL 1522
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLY 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1280-1524 |
4.08e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1280 EKEHSAELERLCSSLEAKHREVvsSLQKKIQEAQQKEEAQLQKclgqvehrvhQKSYHVagyEHELSSLlrekrqevegE 1359
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREV--ERRRKLEEAEKARQAEMDR----------QAAIYA---EQERMAM----------E 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRLDKMK-EEHQQVMAKAREQYEAEERKQraellghlTGELERLQRAHERELETVRQE-----QHKRLEDlrrrhrEQ 1433
Cdd:pfam17380 346 RERELERIRqEERKRELERIRQEEIAMEISR--------MRELERLQMERQQKNERVRQEleaarKVKILEE------ER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1434 ERKLQDLELDLET-RAKDVKARLALLEVQEETARRE----KQQLLDVQRQVA-LKSEEATATHQQLEEAQKEHTHLLQSN 1507
Cdd:pfam17380 412 QRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREmervRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250
....*....|....*..
gi 2462523754 1508 QQLREILDELQARKLKL 1524
Cdd:pfam17380 492 QRRKILEKELEERKQAM 508
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1200-1316 |
4.97e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1200 QIRAEQEA-SLQKLREELESQQKaeraSLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVAT 1278
Cdd:PRK00409 529 ERELEQKAeEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462523754 1279 LEKEHSAELERLCSSLEAKHREvvsslqKKIQEAQQKE 1316
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK------KKKQKEKQEE 636
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1102-1363 |
5.88e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVLEQD-QRHLLESKQEKMQQLREKLCQEEEEEIL---RLHQQKEQSLSSLRERL-----QKAIEEEE 1172
Cdd:pfam17380 332 QAAIYAEQERMAMERERElERIRQEERKRELERIRQEEIAMEISRMReleRLQMERQQKNERVRQELeaarkVKILEEER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1173 ARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLR-EELESQQKAE--RASLEQKNRQMLEQLKEEIEASEKSE 1249
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVErlRQQEEERKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1250 QAALNAAKEKALQQlREQLEGERKEAVatLEKEhsaelerlcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKclgqvEH 1329
Cdd:pfam17380 492 QRRKILEKELEERK-QAMIEEERKRKL--LEKE-----------MEERQKAIYEEERRREAEEERRKQQEMEE-----RR 552
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462523754 1330 RVHQKSYHVAGYEHELSSLLREK---RQEVEGEHERR 1363
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMERERemmRQIVESEKARA 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1187-1322 |
6.28e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1187 RAQVQSSTQADEDQIR--AEQEASLQKLREELESQQKAERAslEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKAlqql 1264
Cdd:PRK09510 80 QRKKKEQQQAEELQQKqaAEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA---- 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1265 rEQLEGERKEAVATLEKEHSAELERLCSSlEAKHREVVSSLQKKIQEAQQKEEAQLQK 1322
Cdd:PRK09510 154 -KRAAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
6.83e-06 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 44.44 E-value: 6.83e-06
10 20 30
....*....|....*....|....*....|.
gi 2462523754 59 PGEWKPCQDITGDIYYFNFANGQSMWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1189-1521 |
7.02e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1189 QVQSSTQADEDQIRAEQEASLQKLREELESqqkaeraslEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLREQL 1268
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES---------EEKNREEVEELKDKYRELRK-TLLANRFSYGPAIDELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1269 EgerkeavaTLEKEHSaELERLCSS---LEAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhv 1338
Cdd:pfam06160 156 A--------EIEEEFS-QFEELTESgdyLEA--REVLEKLEEETDALEELMEdipplyEELKTELpDQLE---------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 agyehELSSLLRE-KRQEVEGEH---ERRLDKMKEEHQQVMA--KAREQYEAEerkqraELLGHLTGELERLQRAHEREL 1412
Cdd:pfam06160 215 -----ELKEGYREmEEEGYALEHlnvDKEIQQLEEQLEENLAllENLELDEAE------EALEEIEERIDQLYDLLEKEV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1413 ETvRQEQHKRLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVAL---KSEEATAT 1489
Cdd:pfam06160 284 DA-KKYVEKNLPEIEDYLEHAEEQNKELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEiveRLEEKEVA 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462523754 1490 H-----------QQLEEAQKEHTHLLQSNQQLREilDELQARK 1521
Cdd:pfam06160 359 YselqeeleeilEQLEEIEEEQEEFKESLQSLRK--DELEARE 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1120-1558 |
8.52e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1120 QRHLLESKQEKMQQLREKLCQEEEE--EILRLHQQKEQSLSSLRERLQKAIE--------------------------EE 1171
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESElkELEKKHQQLCEEKNALQEQLQAETElcaeaeemrarlaarkqeleeilhelES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1172 EARMREEESQRLSWLRAQVQSSTQADEDQIrAEQEASLQKLREE---LESQQKAERASL----EQKNRQMLEQLKEEIEA 1244
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQL-DEEEAARQKLQLEkvtTEAKIKKLEEDIllleDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1245 SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSA--ELERLCSSLEAKH---REVVSSLQKKIQEAQ---QKE 1316
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqELEKAKRKLEGEStdlQEQIAELQAQIAELRaqlAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1317 EAQLQKCLGQVEHRVHQKSyHVAGYEHELSSLLREKRQEVEGEHERR-------------LDKMKEEHQQVMAKAREQYE 1383
Cdd:pfam01576 242 EEELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARnkaekqrrdlgeeLEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1384 AeeRKQRAELLGHLTGELERLQRAHERELETVRQ-------------EQHKR-----------LEDLRRRHREQERKLQD 1439
Cdd:pfam01576 321 L--RSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelteqlEQAKRnkanlekakqaLESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1440 LELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLE----EAQKEHTHLLQSNQQLREILD 1515
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDTQELLQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2462523754 1516 ELQARKLKLESQVDLLQAQSQQLQKHfsLEAEAQKKQHLLREV 1558
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQ--LEEEEEAKRNVERQL 519
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1118-1608 |
1.07e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1118 QDQRHLLESKQEKMQQLREKlCQEEEEEILRLHQQK--------------EQSLSS---LRERLQKAIEEEEARMREEES 1180
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEK-TKLQDENLKELIEKKdhltkeledikmslQRSMSTqkaLEEDLQIATKTICQLTEEKEA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1181 QRLSWLRAQVQSSTqadedqIRAEQEASLQKLREELESQQKaeraSLEqKNRQMLEQLKEEIE--ASEKSEQAALNAAKE 1258
Cdd:pfam05483 336 QMEELNKAKAAHSF------VVTEFEATTCSLEELLRTEQQ----RLE-KNEDQLKIITMELQkkSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1259 KALQQLREQLeGERKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEaqlqkclgQVEHRVHQKSYHV 1338
Cdd:pfam05483 405 VELEELKKIL-AEDEKLL-----DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI--------QLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 AGYEHELSSLLREKRQEVE-GEHERRL----DKMKEEHQQVMAKAREQYE--AEERKQRAELLGHLTgELERLQRAHERE 1411
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIElTAHCDKLllenKELTQEASDMTLELKKHQEdiINCKKQEERMLKQIE-NLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1412 LETVRQEQHKRLEDLR---RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLdvQRQVALKsEEATA 1488
Cdd:pfam05483 550 LESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH--QENKALK-KKGSA 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1489 THQQLE----EAQKEHTHLLQSNQQLREILD----ELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKK-QHLLRE-V 1558
Cdd:pfam05483 627 ENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEmV 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1559 TVEENNASPHfepDLHIEDLRKSLGTNQTKEVSSSLSQSKEDLYLDSLSS 1608
Cdd:pfam05483 707 ALMEKHKHQY---DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKA 753
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1386-1527 |
1.23e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1386 ERKQRAELLGHLTGELERLqrahERELETVRqeqhKRLEDLRRRHREQERKLQDLELDLET---RAKDVKARLAL----- 1457
Cdd:COG1579 18 ELDRLEHRLKELPAELAEL----EDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEveaRIKKYEEQLGNvrnnk 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1458 ----LEVQEETARREKQQL----LDVQRQVALKSEEATATHQQLEEAQKEHTHLLqsnQQLREILDELQARKLKLESQ 1527
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLedeiLELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1275-1520 |
1.36e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1275 AVATLEKEHSAELERLcssleakhREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL---LRE 1351
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1352 KRQEVEgEHERRLDKMKEEHQQVMAKAreqyEAEERKQRAELLGHLTGELERLQRAheRELETVRQEQHKRLEDLRRrhr 1431
Cdd:COG4942 88 LEKEIA-ELRAELEAQKEELAELLRAL----YRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1432 eqerKLQDLElDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEeatathQQLEEAQKEHTHLLQSNQQLR 1511
Cdd:COG4942 158 ----DLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE------KELAELAAELAELQQEAEELE 226
|
....*....
gi 2462523754 1512 EILDELQAR 1520
Cdd:COG4942 227 ALIARLEAE 235
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.68e-05 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 43.26 E-value: 1.68e-05
10 20 30
....*....|....*....|....*....|
gi 2462523754 58 LPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1202-1562 |
1.87e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.52 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1202 RAEQEASLQKLREEL--ESQQKAERASLEQKNRQMLEQLKEEIEAS-EKSEQAALNAAKEKALQQLREQLEG-------- 1270
Cdd:COG5278 85 RAEIDELLAELRSLTadNPEQQARLDELEALIDQWLAELEQVIALRrAGGLEAALALVRSGEGKALMDEIRArllllala 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1271 -ERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1349
Cdd:COG5278 165 lAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALAL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 REKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRR 1429
Cdd:COG5278 245 LLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1430 HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQ 1509
Cdd:COG5278 325 LAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAA 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1510 LREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEE 1562
Cdd:COG5278 405 EAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALA 457
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1154-1351 |
2.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1154 EQSLSSLRERLQKAieeeearmreeeSQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQknrq 1233
Cdd:COG3206 181 EEQLPELRKELEEA------------EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1234 mleqLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHS------AELERLCSSLEAKHREVVSSLQK 1307
Cdd:COG3206 245 ----LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPdvialrAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462523754 1308 KIQEAQQkEEAQLQKCLGQVEHRVHQksyhVAGYEHELSSLLRE 1351
Cdd:COG3206 321 ELEALQA-REASLQAQLAQLEARLAE----LPELEAELRRLERE 359
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1183-1481 |
2.38e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1183 LSWLRAQVQSSTQADEDQIRAEqeasLQKLREELESQQK---AERASLEQKNRQmLEQLKEEIEASEKSEQAALN--AAK 1257
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEE----LEQLREELEQAREeleQLEEELEQARSE-LEQLEEELEELNEQLQAAQAelAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1258 EKALQQLREQLEGERKEaVATLEKEhSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKS 1335
Cdd:COG4372 100 QEELESLQEEAEELQEE-LEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEqlESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1336 yhVAGYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETV 1415
Cdd:COG4372 178 --EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1416 RQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVAL 1481
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
903-1315 |
2.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 903 KASEKEAPEDTVDAGEEGSRREEAAK--EPKKKASALEEGSSDA---SQELEISEHMKEPQLSDSIASDPKSFHGLDFGF 977
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 978 RSRISEHLLDVDvlspvlggACRQAQQplgIEDKDDSQSSQDELQSKQSKGLEERLSPPLPHEERAQSPPRslATEEEPP 1057
Cdd:PTZ00121 1532 EAKKADEAKKAE--------EKKKADE---LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVM 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1058 QGPEGQPEWKeAEELgedsaaslslqlslqRRSTEPVAPPEQLSEaalkamEEAVAQVLEQDQRHLLESKQeKMQQLRek 1137
Cdd:PTZ00121 1599 KLYEEEKKMK-AEEA---------------KKAEEAKIKAEELKK------AEEEKKKVEQLKKKEAEEKK-KAEELK-- 1653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1138 lcqeeeeeilrlhqqKEQSLSSLRERLQKaieeeeaRMREEESQRLSWLRAQVQSSTQADEDQIRAEQEA-SLQKLRE-E 1215
Cdd:PTZ00121 1654 ---------------KAEEENKIKAAEEA-------KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkKAEELKKkE 1711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1216 LESQQKAERA-SLEQKNRQMLEQLK-EEIEASEKSEQAALNAAKEKALQQLREQLEGE----RKEAVATLEKEHSAELER 1289
Cdd:PTZ00121 1712 AEEKKKAEELkKAEEENKIKAEEAKkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKaeeiRKEKEAVIEEELDEEDEK 1791
|
410 420
....*....|....*....|....*.
gi 2462523754 1290 LCSSLEAKHREVVSSLQkKIQEAQQK 1315
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFA-NIIEGGKE 1816
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1086-1359 |
2.65e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.47 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1086 LQRRSTEPVAPPEQLSEAALKAMEEAVAQVLEQDQRHLLESK--QEKMQQLREKLCQEEEE----------EILRLHQQK 1153
Cdd:PLN03229 441 LKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMglQERLENLREEFSKANSQdqlmhpvlmeKIEKLKDEF 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1154 EQSLS------SLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDqiRAEQEASLQKLREELESQQKAERASL 1227
Cdd:PLN03229 521 NKRLSrapnylSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMD--RPEIKEKMEALKAEVASSGASSGDEL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1228 EQKNRQMLEQLKEEIEASE----KSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHRevVS 1303
Cdd:PLN03229 599 DDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSK--IE 676
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1304 SLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGyehelSSLLREKRQEVEGE 1359
Cdd:PLN03229 677 LLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALN-----SSELKEKFEELEAE 727
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1198-1470 |
2.89e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.98 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1198 EDQIRAEQEASLQKLREELESQQKAERASLEQKN-------RQMLEQLKEEIEASEKSEQAALNAAK-----EKALQQLR 1265
Cdd:pfam09731 181 TDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLdaapetpPKLPEHLDNVEEKVEKAQSLAKLVDQykelvASERIVFQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1266 EQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVvSSLQKKIQEAQQKEEAQLQKCLGQVEHrvhqksyhvagyehEL 1345
Cdd:pfam09731 261 QELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI-DQLSKKLAELKKREEKHIERALEKQKE--------------EL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1346 SSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEerkqraellghLTGELERLQRAHERELETVRQEQHkrlED 1425
Cdd:pfam09731 326 DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK-----------LRTELERQAEAHEEHLKDVLVEQE---IE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1426 LRRRHR-------EQERKLQDLELD-LETRAKDVKARLALLEVQEETARREKQ 1470
Cdd:pfam09731 392 LQREFLqdikekvEEERAGRLLKLNeLLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1103-1315 |
2.96e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.92 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1103 AALKAMEEAVAQVLEQdqrhlLESKQEKMQQLrEKLCQEEEEEILRLHQQKEQSLSSLRERLQKAIEEEEARMRE----- 1177
Cdd:PRK11637 75 AQLKKQEEAISQASRK-----LRETQNTLNQL-NKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1178 EESQRLSWLRAQVQSSTQADEDQIraeqeASLQKLREELeSQQKAErasLEQKNRQMLEQLKEEIEASEKSEQA------ 1251
Cdd:PRK11637 149 EESQRGERILAYFGYLNQARQETI-----AELKQTREEL-AAQKAE---LEEKQSQQKTLLYEQQAQQQKLEQArnerkk 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1252 ---ALNAAKEKALQQLRE--QLEGERKEAVATLEKEHSAELERlcsslEAKHREVVsslQKKIQEAQQK 1315
Cdd:PRK11637 220 tltGLESSLQKDQQQLSElrANESRLRDSIARAEREAKARAER-----EAREAARV---RDKQKQAKRK 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1056-1524 |
3.45e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1056 PPQGPEGQPEWKEAEELGEDSAASLSLQLSLQRRSTEpvAPPEQLSEAA--LKAM------EEA--VAQVLEQD---QRH 1122
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ--AAHSQFEQAYqlVRKIagevsrSEAwdVARELLRRlreQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1123 LLESKQEKMQQLREklcqeeeeeiLRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlRAQVQSSTQADEDQIR 1202
Cdd:PRK04863 511 LAEQLQQLRMRLSE----------LEQRLRQQQRAERLLAEFCK--------------------RLGKNLDDEDELEQLQ 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1203 AEQEASLQKLREELESQqkAERASLEqknRQMLEQLKEEIEASEKSEQAALNAakEKALQQLREQLEGERKEAVA----- 1277
Cdd:PRK04863 561 EELEARLESLSESVSEA--RERRMAL---RQQLEQLQARIQRLAARAPAWLAA--QDALARLREQSGEEFEDSQDvteym 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1278 --TLEKEHSAELERlcSSLEAKHRevvsSLQKKIQEAQQKEEAQLQKCLGQVEH-------------RVHQKSYHVAGY- 1341
Cdd:PRK04863 634 qqLLERERELTVER--DELAARKQ----ALDEEIERLSQPGGSEDPRLNALAERfggvllseiyddvSLEDAPYFSALYg 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1342 -------------------------------EHELSSLlREKRQEVE----------GEHERRLDKMKEEhqQVMAK-AR 1379
Cdd:PRK04863 708 parhaivvpdlsdaaeqlagledcpedlyliEGDPDSF-DDSVFSVEelekavvvkiADRQWRYSRFPEV--PLFGRaAR 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1380 EQYEAE---ERKQRAELLGHLTGELERLQRAHERELETVRQ--------EQHKRLEDLRRRHREQERKLQDLE---LDLE 1445
Cdd:PRK04863 785 EKRIEQlraEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavafeaDPEAELRQLNRRRVELERALADHEsqeQQQR 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1446 TRAKDVKARLALL--------------------EVQEETARREKQQLLDVQRQVALKSEEATAthQQLEEAQKEHTHLLQ 1505
Cdd:PRK04863 865 SQLEQAKEGLSALnrllprlnlladetladrveEIREQLDEAEEAKRFVQQHGNALAQLEPIV--SVLQSDPEQFEQLKQ 942
|
570
....*....|....*....
gi 2462523754 1506 SNQQLREILDELQARKLKL 1524
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFAL 961
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1215-1521 |
3.57e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.98 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1215 ELESQQKAERASLEQKNRQMLEqLKEEIeASEKSEQAALnaakEKALQQLREQLEGERKEAVA-TLEKEHSAELERL--- 1290
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAE-LQEQV-TSQSQEQAIL----QRALQDKAAEVEVERMSAKGlQMELSRAQEARRRqqq 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1291 -CSSLEAKHREVVSSLqKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYeHELSSLLREK------RQE-------- 1355
Cdd:pfam07111 395 qTASAEEQLKFVVNAM-SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV-HTIKGLMARKvalaqlRQEscpppppa 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1356 --VEGEHERRLDKMKEEH--------------QQVMAKAREQYEAEeRKQRAELLGHLTGELERLQRAHE---RELETVR 1416
Cdd:pfam07111 473 ppVDADLSLELEQLREERnrldaelqlsahliQQEVGRAREQGEAE-RQQLSEVAQQLEQELQRAQESLAsvgQQLEVAR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1417 QEQHKRLED---LRRRHREQE----RKLQDLELDLETRAKDvkaRLALLEVQEETARREKQQLLDVQRQVALKSEEATAT 1489
Cdd:pfam07111 552 QGQQESTEEaasLRQELTQQQeiygQALQEKVAEVETRLRE---QLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
330 340 350
....*....|....*....|....*....|..
gi 2462523754 1490 HQQLEEAQKEHTHllQSNQQLREILDELQARK 1521
Cdd:pfam07111 629 NQELRRLQDEARK--EEGQRLARRVQELERDK 658
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1192-1392 |
3.73e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.79 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1192 SSTQADEDQIRAEQeASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGE 1271
Cdd:pfam15709 329 EQEKASRDRLRAER-AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1272 RKEAVatlekEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgqvehrvhqksyhvagyehelssllRE 1351
Cdd:pfam15709 408 RKQRL-----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ----------------------------RQ 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462523754 1352 KRQEVE-GEHERRLDKMKEEH------QQVMAKAREQYEAEERKQRAE 1392
Cdd:pfam15709 455 KELEMQlAEEQKRLMEMAEEErleyqrQKQEAEEKARLEAEERRQKEE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1098-1425 |
3.79e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1098 EQLSEAALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKAieEEEARMRE 1177
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--EEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1178 EESQRLSWLRAQVQSSTQADEDQIRAEQEA------SLQKLREELESQQKAERAS------LEQKNRQMLEQLkEEIEAS 1245
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATerrledLEEQIEELSEDI-ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1246 EKSEQAALNAAKE--KALQQLREQLEGERKEAVATLEK------EHSAELERLCSSLEAKhREVVSSLQKKIQEAQQKEE 1317
Cdd:TIGR02168 861 IEELEELIEELESelEALLNERASLEEALALLRSELEElseelrELESKRSELRRELEEL-REKLAQLELRLEGLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1318 AQLQKC--LGQVEHRVHQKSYhvagyehelssllrEKRQEVEGEHERRLDKMKEEHQQ---VMAKAREQYEAEErkqraE 1392
Cdd:TIGR02168 940 NLQERLseEYSLTLEEAEALE--------------NKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELK-----E 1000
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462523754 1393 LLGHLTGELERLQRAHERELETVRQ---EQHKRLED 1425
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEidrEARERFKD 1036
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
4.17e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.20 E-value: 4.17e-05
10 20 30
....*....|....*....|....*....|.
gi 2462523754 57 PLPGEWKPCQDITGDIYYFNFANGQSMWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1181-1567 |
4.39e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1181 QRLSWLRAQVQSSTQaDEDQIRAEQEaslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKseQAALNAAKEKA 1260
Cdd:TIGR00606 591 DRLAKLNKELASLEQ-NKNHINNELE---SKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSK--QRAMLAGATAV 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1261 LQQLREQLEGERKEAVATLEK--EHSAELERLCSSLEAKHReVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQksyhV 1338
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRvfQTEAELQEFISDLQSKLR-LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI----I 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 AGYEHELSSLlREKRQEVEGEHERRLDKMKEEHQQVmakarEQYEAEErkQRAELLGHLTGELERLQrahereletvrqe 1418
Cdd:TIGR00606 740 DLKEKEIPEL-RNKLQKVNRDIQRLKNDIEEQETLL-----GTIMPEE--ESAKVCLTDVTIMERFQ------------- 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1419 qhKRLEDLRRRHREQERKLQDLELDLEtrakdvkarlalleVQEetARREKQQLLDVQRQVALKSEEatatHQQLEEAQK 1498
Cdd:TIGR00606 799 --MELKDVERKIAQQAAKLQGSDLDRT--------------VQQ--VNQEKQEKQHELDTVVSKIEL----NRKLIQDQQ 856
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1499 EHTHLLQSNqqlreiLDELQARKLKLESQVDLLQAQSQQlqkhfsLEAEAQKKQHLLREVTVEENNASP 1567
Cdd:TIGR00606 857 EQIQHLKSK------TNELKSEKLQIGTNLQRRQQFEEQ------LVELSTEVQSLIREIKDAKEQDSP 913
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1195-1267 |
4.59e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 45.55 E-value: 4.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1195 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1267
Cdd:COG0711 47 KEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAE 119
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1054-1314 |
5.32e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1054 EEPPQGPEGQPEWKEAEELGEDSAASLSLQLSlQRRSTEPVAPPEQlsEAALKAMEEAVAQVleqdqrhlleSKQEKMQQ 1133
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELE-QKLSVADAARRQF--EKAYELVCKIAGEV----------ERSQAWQT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1134 LREKLCQeeeeeiLRLHQQKEQSLSSLRERLQKAieeeearmreeeSQRLswlRAQVQSSTQADEDQIRAEQEASLQKLR 1213
Cdd:COG3096 497 ARELLRR------YRSQQALAQRLQQLRAQLAEL------------EQRL---RQQQNAERLLEEFCQRIGQQLDAAEEL 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1214 EELESQQKAERASLEQKN----------RQMLEQLKEEIEASEKSEQAALNAAkeKALQQLREQLEGERKEAVA------ 1277
Cdd:COG3096 556 EELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPAWLAAQ--DALERLREQSGEALADSQEvtaamq 633
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462523754 1278 -TLEKEHSAELERlcSSLEAKHREvvssLQKKIQEAQQ 1314
Cdd:COG3096 634 qLLEREREATVER--DELAARKQA----LESQIERLSQ 665
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1199-1487 |
5.72e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRA--EQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKsEQAALNAAKEKA---LQQLREQLE---G 1270
Cdd:pfam00038 18 DKVRFleQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTV-ERARLQLELDNLrlaAEDFRQKYEdelN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1271 ERKEA---VATLEKE-HSAELERLcssleakhrevvsSLQKKIQEAQqkEEAQLQKCLGQVEHRvhqksyhvagyehELS 1346
Cdd:pfam00038 97 LRTSAendLVGLRKDlDEATLARV-------------DLEAKIESLK--EELAFLKKNHEEEVR-------------ELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1347 SLLREKRQEVEGEHERRLDKmkeehQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKrLEDL 1426
Cdd:pfam00038 149 AQVSDTQVNVEMDAARKLDL-----TSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEE-ITEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1427 RRR----------HREQ----ERKLQDLELDLETRAKDVKARLALLEVQ-----EETAR--REKQQLLDVqrQVALKSEE 1485
Cdd:pfam00038 223 RRTiqsleielqsLKKQkaslERQLAETEERYELQLADYQELISELEAElqetrQEMARqlREYQELLNV--KLALDIEI 300
|
..
gi 2462523754 1486 AT 1487
Cdd:pfam00038 301 AT 302
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1199-1318 |
6.14e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRAEQEASLQKLREELeSQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAKE----KALQQlREQLEGERKE 1274
Cdd:COG1842 29 DQAIRDMEEDLVEARQAL-AQVIANQKRLERQ----LEELEAEAEKWEEKARLALEKGREdlarEALER-KAELEAQAEA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462523754 1275 AVATLEkEHSAELERLcssleakhREVVSSLQKKIQEAQQKEEA 1318
Cdd:COG1842 103 LEAQLA-QLEEQVEKL--------KEALRQLESKLEELKAKKDT 137
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1199-1392 |
7.35e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 48.29 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRAEQEASLQ--KLREELESQQKAERASLEQK----NRQMLEQLKEEIEASEKSEQAALNAAKEKAL----QQLREQL 1268
Cdd:NF012221 1532 DNVVATSESSQQadAVSKHAKQDDAAQNALADKEraeaDRQRLEQEKQQQLAAISGSQSQLESTDQNALetngQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1269 EGERKEAVATLEK------------EHSAEL---------ERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQkclgQV 1327
Cdd:NF012221 1612 LEESRAVTKELTTlaqgldaldsqaTYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQ----KV 1687
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1328 EHRVHQKSYHVA-GYEHELSSLLREKRQEVEGEhERRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1392
Cdd:NF012221 1688 KDAVAKSEAGVAqGEQNQANAEQDIDDAKADAE-KRKDDALAKQNEAQQAESDANAAANDAQSRGE 1752
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1372-1501 |
7.89e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1372 QQVMAKAREQYEAEERK-----QRAEllghltgELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLEt 1446
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKlneliASLE-------ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE- 572
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1447 rakdVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQKEHT 1501
Cdd:PRK00409 573 ----KEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1349-1566 |
8.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1349 LREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEER-KQRAELLGHLTGELERLQR---AHERELETVRQEQHKRLE 1424
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAelaELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1425 DLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQValksEEATATHQQLEEAQKEHTHLL 1504
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1505 QSNQQLREILDELQARKLK----LESQVDLLQAQSQQlqkhfsLEAEAQKKQHLLREVTVEENNAS 1566
Cdd:COG4942 181 AELEEERAALEALKAERQKllarLEKELAELAAELAE------LQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1183-1526 |
8.87e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1183 LSWLRAQ-VQSSTQADEDQIRAE-QEASLQKlreeleSQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAakEKA 1260
Cdd:PRK10929 9 MAWLLSWgAYAATAPDEKQITQElEQAKAAK------TPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNF--PKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1261 LQQLREQLEGERKE--------AVATLEKE------HSAELERLCSSLEAKHREVVSSLQkkiQEAQQKEEAqlQKCLGQ 1326
Cdd:PRK10929 81 SAELRQQLNNERDEprsvppnmSTDALEQEilqvssQLLEKSRQAQQEQDRAREISDSLS---QLPQQQTEA--RRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1327 VEHRVH-------------------QKSYHVAGY-EHELSSLLREKRQEVEgehERRLDKMKEEHQQVMAK--------- 1377
Cdd:PRK10929 156 IERRLQtlgtpntplaqaqltalqaESAALKALVdELELAQLSANNRQELA---RLRSELAKKRSQQLDAYlqalrnqln 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1378 AREQYEAEERKQRAELLGHLTGEL-----ERLQRahERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLET---RAK 1449
Cdd:PRK10929 233 SQRQREAERALESTELLAEQSGDLpksivAQFKI--NRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTlreQSQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1450 DVKARLALLE-VQEETAR---REKQQLLD-------VQRqvaLKSEEATATHQQLEEAQKEHTHLLQSNQQlrEILDE-L 1517
Cdd:PRK10929 311 WLGVSNALGEaLRAQVARlpeMPKPQQLDtemaqlrVQR---LRYEDLLNKQPQLRQIRQADGQPLTAEQN--RILDAqL 385
|
....*....
gi 2462523754 1518 QARKLKLES 1526
Cdd:PRK10929 386 RTQRELLNS 394
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1385-1591 |
9.81e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1385 EERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEET 1464
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1465 ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDEL-------QARKLKLESQVDLLQAQSQQ 1537
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELqseiaerEEELKELEEQLESLQEELAA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462523754 1538 LQKHFSLEAEAQKKQHlLREVTVEENNASPHFEPDLHIEDLRKSLGTNQTKEVS 1591
Cdd:COG4372 169 LEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1197-1507 |
1.08e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1197 DEDQIRAEQEASlQKLREELESQQKAERASLEQKNRQMLEQ---------LKEEIEASEKSEQAALN---AAKEKALQQL 1264
Cdd:pfam02029 1 IEDEEEAARERR-RRAREERRRQKEEEEPSGQVTESVEPNEhnsyeedseLKPSGQGGLDEEEAFLDrtaKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1265 REQLEGE----------------RKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQlqkclgQVE 1328
Cdd:pfam02029 80 QEALERQkefdptiadekesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVR------QAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1329 HRVHQKSYHVAgyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAkaREQYEAEERKQRAELLGHLTGELERLQRAH 1408
Cdd:pfam02029 154 EEGEEEEDKSE--EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLD--QKRGHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1409 ERELETVRQEQH------KRLEDLRRRHREQER--------KLQDLELDLETRAKDVKARLALLEvqEETARREKQQLld 1474
Cdd:pfam02029 230 LSQSQEREEEAEvfleaeQKLEELRRRRQEKESeefeklrqKQQEAELELEELKKKREERRKLLE--EEEQRRKQEEA-- 305
|
330 340 350
....*....|....*....|....*....|...
gi 2462523754 1475 vQRQVAlKSEEATATHQQLEEAQKEHTHLLQSN 1507
Cdd:pfam02029 306 -ERKLR-EEEEKRRMKEEIERRRAEAAEKRQKL 336
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1345-1499 |
1.34e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1345 LSSLLREKRQEV-EGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRaellghltgELERLQRAH-ERELETVRQEQHKR 1422
Cdd:COG2268 186 LDALGRRKIAEIiRDARIAEAEAERETEIAIAQANREAEEAELEQER---------EIETARIAEaEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1423 LEDLRRR-----HREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL--DVQRQVALKSEEATATHQQlEE 1495
Cdd:COG2268 257 AETARAEaeaayEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaEAEKQAAEAEAEAEAEAIR-AK 335
|
....
gi 2462523754 1496 AQKE 1499
Cdd:COG2268 336 GLAE 339
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1305-1476 |
1.95e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1305 LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGY------------------------EHELSSLLREKrqEVEGE 1359
Cdd:cd16269 107 CKQNEEASSKRCQALLQELSAPLEEKISQGSYSVpGGYqlyledreklvekyrqvprkgvkaEEVLQEFLQSK--EAEAE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1360 HERRLDKMKEEHQQVMAKAREQYEAEErkQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQD 1439
Cdd:cd16269 185 AILQADQALTEKEKEIEAERAKAEAAE--QERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALE 262
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462523754 1440 LELDLETRakdvkarlALLEVQEETARREKQQLLDVQ 1476
Cdd:cd16269 263 SKLKEQEA--------LLEEGFKEQAELLQEEIRSLK 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1296-1472 |
2.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1296 AKHREVVSSLQKKIQEAQQkEEAQLQKCLGQVEHRVHqksyhvagyehELSSLLREKRQEVEgEHERRLDKMKEehQQVM 1375
Cdd:COG1579 20 DRLEHRLKELPAELAELED-ELAALEARLEAAKTELE-----------DLEKEIKRLELEIE-EVEARIKKYEE--QLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1376 AKAREQYEAeerkqraellghLTGELERLQRAHErELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARL 1455
Cdd:COG1579 85 VRNNKEYEA------------LQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*..
gi 2462523754 1456 ALLEVQEETARREKQQL 1472
Cdd:COG1579 152 AELEAELEELEAEREEL 168
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1344-1525 |
2.95e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 44.29 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1344 ELSSLLREKRQEVEGEH--ERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRaHERELETVRQEQHK 1421
Cdd:pfam04012 33 DMQSELVKARQALAQTIarQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEK-QAEALETQLAQQRS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1422 RLEDLRRRHREQERKLQDLELDLETrakdVKARLALLEVQEETArrekqqlldvQRQVALKSEEATATHQQLEEAQKEht 1501
Cdd:pfam04012 112 AVEQLRKQLAALETKIQQLKAKKNL----LKARLKAAKAQEAVQ----------TSLGSLSTSSATDSFERIEEKIEE-- 175
|
170 180
....*....|....*....|....
gi 2462523754 1502 hlLQSNQQLREILDELQARKLKLE 1525
Cdd:pfam04012 176 --REARADAAAELASAVDLDAKLE 197
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1243-1527 |
3.09e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1243 EASEKSEQAAlnaAKEKALQQLREQLEGERKEAVAtLEKEHsAELERLCSSLEAKHREVVSSLQKkIQEAQQKEEAqlqk 1322
Cdd:COG3096 279 ERRELSERAL---ELRRELFGARRQLAEEQYRLVE-MAREL-EELSARESDLEQDYQAASDHLNL-VQTALRQQEK---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1323 clgqvehrvhqksyhVAGYEHELSSLlrekrqevegehERRLdkmkEEHQQVMAKAREQY-EAEERKQRAEL-LGHLTGE 1400
Cdd:COG3096 349 ---------------IERYQEDLEEL------------TERL----EEQEEVVEEAAEQLaEAEARLEAAEEeVDSLKSQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1401 LERLQRA----HERELEtVRQ-----EQHKRL-----------EDLRRRHREQERKLQDLELDLETRAKDVKArlallev 1460
Cdd:COG3096 398 LADYQQAldvqQTRAIQ-YQQavqalEKARALcglpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADA------- 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1461 qeetARREKQQLLDVQRQVA--LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARklkLESQ 1527
Cdd:COG3096 470 ----ARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQR---LRQQ 531
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1116-1452 |
3.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1116 LEQDQRHLLESKQEKMQQLREKlcQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswLRAQVQSSTQ 1195
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEK--QNEIEKLKKENQSYKQEIKNLESQIND-------------------LESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1196 adEDQIRAEQEASLQKLREELESQQKAERASLEqKNRQMLEQLKEEIEASEKsEQAALNAAKEKALQQLrEQLEGERKEA 1275
Cdd:TIGR04523 406 --LNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKDLTNQDSVKEL-IIKNLDNTRESLETQL-KVLSRSINKI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1276 VATLEKEhSAELERLCSSLEAKHREV------VSSLQKKIQEAQQKEEaqlqkclgQVEHRVHQKSYHVAGYEHELSS-- 1347
Cdd:TIGR04523 481 KQNLEQK-QKELKSKEKELKKLNEEKkeleekVKDLTKKISSLKEKIE--------KLESEKKEKESKISDLEDELNKdd 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1348 --LLREKRQEVEGEHERRLDKMKEEHQQVMAKARE------QYEAEERKQRAELLghltgELERLQRAHERELETVRQEq 1419
Cdd:TIGR04523 552 feLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIE-----EKEKKISSLEKELEKAKKE- 625
|
330 340 350
....*....|....*....|....*....|...
gi 2462523754 1420 HKRLEdlrrrhrEQERKLQDLELDLETRAKDVK 1452
Cdd:TIGR04523 626 NEKLS-------SIIKNIKSKKNKLKQEVKQIK 651
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1292-1499 |
3.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1292 SSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHqksyhvagyehelssllrEKRQEVEGEHERRLDKMKEEH 1371
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH------------------KLRNEFEKELRERRNELQKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1372 QQVMAKareqyeaEER-KQRAELLGHLTGELErlqrAHERELETVRQEQHKRLEDLRRRHREQERKLQDL-ELDLEtrak 1449
Cdd:PRK12704 89 KRLLQK-------EENlDRKLELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAE---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1450 dvKARLALLEVQEETARREKQQLLdvqRQValkSEEATathqqlEEAQKE 1499
Cdd:PRK12704 154 --EAKEILLEKVEEEARHEAAVLI---KEI---EEEAK------EEADKK 189
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1183-1708 |
3.82e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1183 LSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQqkaerasLEQKNRQMLeQLKEEIEaseKSEQAALNAAKEKALQ 1262
Cdd:pfam10174 164 LEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL-------LDQKEKENI-HLREELH---RRNQLQPDPAKTKALQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1263 QLREQLE---GERKEAVATLEKE-----HSAELERLCSSLEAKHREVVSSLQK----KIQEAQQ---KEEAQLQKCLGQV 1327
Cdd:pfam10174 233 TVIEMKDtkiSSLERNIRDLEDEvqmlkTNGLLHTEDREEEIKQMEVYKSHSKfmknKIDQLKQelsKKESELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1328 EHRVHQKS---YHVAGYEHELSSllREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE--AEERkqraellGHLTGELE 1402
Cdd:pfam10174 313 ETLTNQNSdckQHIEVLKESLTA--KEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQdlTEEK-------STLAGEIR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1403 RLQR---AHERELETVrqeqHKRLEDLRRRHREQERKLQDLE---LDLETRAKDVKARLALLEvqeeTARREKQQLLDvq 1476
Cdd:pfam10174 384 DLKDmldVKERKINVL----QKKIENLQEQLRDKDKQLAGLKervKSLQTDSSNTDTALTTLE----EALSEKERIIE-- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1477 rqvALKSEEATATHQQLEEAQKehthLLQSNQQLREILDELQARKLKLESQVDLLQAQSQ--------QLQKHFSLEAEA 1548
Cdd:pfam10174 454 ---RLKEQREREDRERLEELES----LKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassglkKDSKLKSLEIAV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1549 QKK---------QHLLREVTVEENNASPHFepDLHIEDLRKSLGTNQTKevsSSLSQSKEDLYLDSLSSHNVWHLLSAEG 1619
Cdd:pfam10174 527 EQKkeecsklenQLKKAHNAEEAVRTNPEI--NDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKNDKDKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1620 VAlrSAKEFLVQQTRSMRRRQTALKAAQQHWRHELAS-------AQEVAKDPPGIKALEDMRKNLEKETRHLDEMKSAMR 1692
Cdd:pfam10174 602 IA--ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
570
....*....|....*.
gi 2462523754 1693 KGHNLLKKKEEKLNQL 1708
Cdd:pfam10174 680 STQQSLAEKDGHLTNL 695
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1210-1312 |
4.00e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 43.29 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1210 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAvatlEKEhsaeler 1289
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKE-LQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQQEA----QQD------- 109
|
90 100
....*....|....*....|...
gi 2462523754 1290 lcssLEAKHREVVSSLQKKIQEA 1312
Cdd:COG2825 110 ----LQKRQQELLQPILEKIQKA 128
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1105-1467 |
4.52e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1105 LKAMEEAVAQVLEQDQRHLL----ESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearMREEES 1180
Cdd:pfam15558 37 LRRRDQKRQETLERERRLLLqqsqEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAED--------QENQRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1181 QRLSWLRAQVQSSTQADEDQIRaEQEASLQKLRE--ELESQQKAERASLEQKNRQMLEQLKeeIEASEKSEQAALNAAKE 1258
Cdd:pfam15558 109 EKLERARQEAEQRKQCQEQRLK-EKEEELQALREqnSLQLQERLEEACHKRQLKEREEQKK--VQENNLSELLNHQARKV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1259 KALQQLREQLEGERKeavaTLEKEHSAELERLCSSLEAKHREvvsslqkkIQEAQQKEEAQLQKclgqvehrvhqksyhv 1338
Cdd:pfam15558 186 LVDCQAKAEELLRRL----SLEQSLQRSQENYEQLVEERHRE--------LREKAQKEEEQFQR---------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 agyehelsslLREKRQEVEGEHERRLDKMKEEHQQVMAKAReQYEAEERKQRAELLGHLTGELERLQRAHERELEtvRQE 1418
Cdd:pfam15558 238 ----------AKWRAEEKEEERQEHKEALAELADRKIQQAR-QVAHKTVQDKAQRARELNLEREKNHHILKLKVE--KEE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1419 QHKR---LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLE-VQEETARR 1467
Cdd:pfam15558 305 KCHRegiKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREkVREETNNR 357
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1198-1322 |
4.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1198 EDQIRAEQEA--SLQKLREELESQQKAERASLEQKNRQM--------LEQLKEEIEASEKSEQAAlnaakEKALQQLREQ 1267
Cdd:COG1579 44 EARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeYEALQKEIESLKRRISDL-----EDEILELMER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1268 LEgERKEAVATLEKEHsAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1322
Cdd:COG1579 119 IE-ELEEELAELEAEL-AELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1255-1499 |
4.90e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1255 AAKEKALQQLREQLEgERKEAVATLEKEhSAELERLcssLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQk 1334
Cdd:PRK04863 782 AAREKRIEQLRAERE-ELAERYATLSFD-VQKLQRL---HQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALAD- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1335 syhVAGYEHELSSLLREKRQEVEG--EHERRLDKMKEEH-QQVMAKAREQ-YEAEERKQRAELLGHLTGELERLQ---RA 1407
Cdd:PRK04863 856 ---HESQEQQQRSQLEQAKEGLSAlnRLLPRLNLLADETlADRVEEIREQlDEAEEAKRFVQQHGNALAQLEPIVsvlQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1408 HERELETVRQeQHKRLEDLRRRHREQERKLQDL-----ELDLETRAKDV----------KARLALLEVQEETAR---REK 1469
Cdd:PRK04863 933 DPEQFEQLKQ-DYQQAQQTQRDAKQQAFALTEVvqrraHFSYEDAAEMLaknsdlneklRQRLEQAEQERTRAReqlRQA 1011
|
250 260 270
....*....|....*....|....*....|..
gi 2462523754 1470 QQLLD--VQRQVALKSeEATATHQQLEEAQKE 1499
Cdd:PRK04863 1012 QAQLAqyNQVLASLKS-SYDAKRQMLQELKQE 1042
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1124-1712 |
5.11e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1124 LESKQEKMQQLREKLcqeeeeeilrlhQQKEQSLSSLRERLQKaieeeearmREEESQRLSWLRAQVQSSTqadeDQIRA 1203
Cdd:TIGR04523 182 KLNIQKNIDKIKNKL------------LKLELLLSNLKKKIQK---------NKSLESQISELKKQNNQLK----DNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1204 EQEaSLQKLREELESQQKaERASLEQKNRQMLEQLKEEIEASEKSEQaaLNAAKEKALQQLREQLEGERKEAVATLEKEH 1283
Cdd:TIGR04523 237 KQQ-EINEKTTEISNTQT-QLNQLKDEQNKIKKQLSEKQKELEQNNK--KIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1284 SAELErlcssleakhrevvsSLQKKIQEAQqKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSL---LREKRQEVEgeh 1360
Cdd:TIGR04523 313 KSELK---------------NQEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKqreLEEKQNEIE--- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1361 erRLDKMKEEHQQVMAKAREQYEAEERK--QRAELLGHLTGELERLQRAHEreletVRQEQHKRLEDLRRRHREQERKLQ 1438
Cdd:TIGR04523 374 --KLKKENQSYKQEIKNLESQINDLESKiqNQEKLNQQKDEQIKKLQQEKE-----LLEKEIERLKETIIKNNSEIKDLT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1439 DLELDLETRAKDVKARLALLEVQEETARRE----KQQLLDVQRQVALKSEEA---TATHQQLEEAQKEhthLLQSNQQLR 1511
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKSKEKELkklNEEKKELEEKVKD---LTKKISSLK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1512 EILDELQARKLKLESQVDllqaqsqqlqkhfSLEAEAQKKqhllrevtveennasphfEPDLHIEDLRKSLGTNQTKevs 1591
Cdd:TIGR04523 524 EKIEKLESEKKEKESKIS-------------DLEDELNKD------------------DFELKKENLEKEIDEKNKE--- 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1592 ssLSQSKEDlyldslsshnvwhllsaegvalrsakeflvqqtrsmrrrQTALKAAQQHwrhelasAQEVAKDppgikaLE 1671
Cdd:TIGR04523 570 --IEELKQT---------------------------------------QKSLKKKQEE-------KQELIDQ------KE 595
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2462523754 1672 DMRKNLEKETRHLDEMKSAMRKGHNLLKKKEEKLNQLESSL 1712
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1364-1527 |
5.42e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 43.22 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1364 LDKMKEEHQQVMAKAREQY-----EAEERKQRAEL-LGHLTGELERLQRAHERELETVRQeQHKRLEDLRRRHREQERKL 1437
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYvqeceEIERRRQELASrYTQQTAELQTQLLQKEKEQASLKK-ELQALRPFAKLKESQEREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1438 QDLELDLET--RAKDVKARLALLEVQEETARREKQ-QLLDVQRQVALKSEEATATHQQLEEAQK----EHTHLL-QSNQQ 1509
Cdd:pfam14988 88 QDLEEEKEKvrAETAEKDREAHLQFLKEKALLEKQlQELRILELGERATRELKRKAQALKLAAKqalsEFCRSIkRENRQ 167
|
170 180
....*....|....*....|....*
gi 2462523754 1510 LREIL-------DELQARKLKLESQ 1527
Cdd:pfam14988 168 LQKELlqliqetQALEAIKSKLENR 192
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1214-1529 |
5.71e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1214 EELESQQKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKA--LQQLREQLEGERKEAVATLEKehsaeLERLC 1291
Cdd:pfam09728 3 ARELMQLLNKLDSPEEKL-AALCKKYAELLEEMKRLQKDLKKLKKKQdqLQKEKDQLQSELSKAILAKSK-----LEKLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1292 SSLEAKHREVVSSLQKKIQEAQQKEE---AQLQKCLGQVEHRVHQKSYHVAGYEHElSSLLREKRQEVEGEHERR----- 1363
Cdd:pfam09728 77 RELQKQNKKLKEESKKLAKEEEEKRKelsEKFQSTLKDIQDKMEEKSEKNNKLREE-NEELREKLKSLIEQYELRelhfe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1364 -LDKMKEEHQQ-VMAKAREQYEAEERKQRaellghltgelerlqrahERELETVRQEQhKRLEDLRrrhrEQERKLQD-L 1440
Cdd:pfam09728 156 kLLKTKELEVQlAEAKLQQATEEEEKKAQ------------------EKEVAKARELK-AQVQTLS----ETEKELREqL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1441 ELDLEtRAKDVKARLALLEVQEETARREKQQLLDVQRQValkSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1520
Cdd:pfam09728 213 NLYVE-KFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKL---EKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKK 288
|
....*....
gi 2462523754 1521 KLKLESQVD 1529
Cdd:pfam09728 289 LEKLENLCR 297
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1210-1315 |
6.20e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.80 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1210 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1289
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK-------- 87
|
90 100
....*....|....*....|....*.
gi 2462523754 1290 lcssleaKHREVVSSLQKKIQEAQQK 1315
Cdd:smart00935 88 -------RQQEELQKILDKINKAIKE 106
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1121-1554 |
6.29e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1121 RHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQSLSSLR--ERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADE 1198
Cdd:pfam09731 33 RDFFEEYIPYGEEVVLYALGEDPPLAPKPKTFRPLQPSVVSavTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNA------AKEKALQQLREQLEGER 1272
Cdd:pfam09731 113 AEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEAsdtaeiSREKATDSALQKAEALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1273 KEAVATLEKEHSAELERLcSSLEAKHREVVSSLQKKIQEAQQKEEA--QLQKCLGQVEHRVH----QKSYHVAGYEHELS 1346
Cdd:pfam09731 193 EKLKEVINLAKQSEEEAA-PPLLDAAPETPPKLPEHLDNVEEKVEKaqSLAKLVDQYKELVAseriVFQQELVSIFPDII 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1347 SLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKqraellghltgeLERLQRAHERELETVRQEQHKRLEDL 1426
Cdd:pfam09731 272 PVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKH------------IERALEKQKEELDKLAEELSARLEEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1427 RRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLdvqrqvalkseeatathQQLEEAQKEHTHLLQS 1506
Cdd:pfam09731 340 RAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLV-----------------EQEIELQREFLQDIKE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462523754 1507 nqqlrEILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHL 1554
Cdd:pfam09731 403 -----KVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQL 445
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1194-1474 |
6.79e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1194 TQADEDQIRAEQEASLQKLREELESQQKAERasleqKNRQMLEQLKEEIEASEKSEQAALNAAKEkaLQQLREQLEGERK 1273
Cdd:pfam05667 217 AAAQEWEEEWNSQGLASRLTPEEYRKRKRTK-----LLKRIAEQLRSAALAGTEATSGASRSAQD--LAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1274 EAVATLEKEHSAELERLCSSLEAKHREVVSSLQKK----IQEAQQKEEAQLQKCLGQVEHRVHQksyhvagYEHELSSLL 1349
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVEteeeLQQQREEELEELQEQLEDLESSIQE-------LEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 REKRQ-EVEGEHERRLDKMKEEHQQVMAKAREQY-EAEER--------KQRAELLGHLTGELERLQRAHERELETVRQEQ 1419
Cdd:pfam05667 363 SSIKQvEEELEELKEQNEELEKQYKVKKKTLDLLpDAEENiaklqalvDASAQRLVELAGQWEKHRVPLIEEYRALKEAK 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523754 1420 HKRLEdlrrrhrEQERKLQDLEldlETRAKdvkarlaLLEVQEETARRE--KQQLLD 1474
Cdd:pfam05667 443 SNKED-------ESQRKLEEIK---ELREK-------IKEVAEEAKQKEelYKQLVA 482
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
1199-1270 |
7.27e-04 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 42.56 E-value: 7.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462523754 1199 DQIRAEQEASLQKLREELESQQKaERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKeKALQQLREQLEG 1270
Cdd:pfam10211 118 EQGKAELEKKIADLEEEKEELEK-QVAELKAKCEAIEKREEERRQAEEKKHAEEIAFLK-KTNQQLKAQLER 187
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1067-1455 |
9.00e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELGEDSAASLSLQLSLQRRSTEPVAPPEQLSEAALKAMEEAVAQ---VLEQDQRHLLES-------KQEKMQQLRE 1136
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdEKQSEKDKKNKAlaerkdsANERLNSLEA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1137 KLCQEEEEEILRLHQQKEQSLSSLRERLQKaiEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKL--RE 1214
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREARTEKQAY--WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1215 ELESQQKAERASLEQK------NRQML---EQLKEEIEASEKSEQAALNAAKEKALQQLREQL---EGERKEAVATLEKE 1282
Cdd:pfam12128 768 DVIAKLKREIRTLERKieriavRRQEVlryFDWYQETWLQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEME 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1283 HSAeLERLCSSLEAKHREVVSSLQK--KIQEAQQKEEAQLQ--KCLGQVEHRVHQKSYHVAGYEHELS---SLLREKRQE 1355
Cdd:pfam12128 848 RKA-SEKQQVRLSENLRGLRCEMSKlaTLKEDANSEQAQGSigERLAQLEDLKLKRDYLSESVKKYVEhfkNVIADHSGS 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1356 VEGEHERRLdkMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER 1435
Cdd:pfam12128 927 GLAETWESL--REEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDLTEFYDVLADFDRRIASFSR 1004
|
410 420
....*....|....*....|...
gi 2462523754 1436 KLQ---DLELDLEtRAKDVKARL 1455
Cdd:pfam12128 1005 ELQrevGEEAFFE-GVSESAVRI 1026
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1155-1494 |
9.18e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1155 QSLSSLRERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREELESQ---QKAERASLEQKN 1231
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1232 RQMLEqlkeEIEASEKSEQAALNAAKEKALQQLREQLEGERKeAVATLEKEHSAELERLcsSLEAKHREVvssLQKKIQE 1311
Cdd:pfam07111 139 QRELE----EIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEK-SLNSLETKRAGEAKQL--AEAQKEAEL---LRKQLSK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1312 AQQKEEAQ------LQKCLG-QVEHRVHQKSYHVAGYEH-ELSSLLREKRQEVEGEHE---------RRLDKMKEEHQQV 1374
Cdd:pfam07111 209 TQEELEAQvtlvesLRKYVGeQVPPEVHSQTWELERQELlDTMQHLQEDRADLQATVEllqvrvqslTHMLALQEEELTR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1375 MAKAREQYEAEERKQRAELLGH-------LTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ---ERKLQDLELDL 1444
Cdd:pfam07111 289 KIQPSDSLEPEFPKKCRSLLNRwrekvfaLMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailQRALQDKAAEV 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1445 ETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLE 1494
Cdd:pfam07111 369 EVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1227-1521 |
1.00e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1227 LEQKNRQMLEQLKEEIEASEKSeQAALNAAKEKaLQQLREQLEGERK---EAVATLEKEHS------AELERLCSS---L 1294
Cdd:PRK04778 117 IEEDIEQILEELQELLESEEKN-REEVEQLKDL-YRELRKSLLANRFsfgPALDELEKQLEnleeefSQFVELTESgdyV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1295 EAkhREVVSSLQKKIQEAQQKEE------AQLQKCL-GQVEhrvhqksyhvagyehELSSLLREkrQEVEGEH------E 1361
Cdd:PRK04778 195 EA--REILDQLEEELAALEQIMEeipellKELQTELpDQLQ---------------ELKAGYRE--LVEEGYHldhldiE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1362 RRLDKMKEEHQQVMAkareQYEAEERKQRAELLGHLTGELERLQRAHERELETvRQEQHKRLEDLRRRHREQERKLQDLE 1441
Cdd:PRK04778 256 KEIQDLKEQIDENLA----LLEELDLDEAEEKNEEIQERIDQLYDILEREVKA-RKYVEKNSDTLPDFLEHAKEQNKELK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1442 LDLETrakdVKARLALLEVQEETARREKQQLLDVQRQVaLKSEEATATHQ---------------QLEEAQKEHTHLLQS 1506
Cdd:PRK04778 331 EEIDR----VKQSYTLNESELESVRQLEKQLESLEKQY-DEITERIAEQEiayselqeeleeilkQLEEIEKEQEKLSEM 405
|
330
....*....|....*
gi 2462523754 1507 NQQLREilDELQARK 1521
Cdd:PRK04778 406 LQGLRK--DELEARE 418
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1401-1583 |
1.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1401 LERLQRAHER--ELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDV--Q 1476
Cdd:COG1579 9 LLDLQELDSEldRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1477 RQV-ALKSEEATATHQQ--LEEAQKEHTHLLqsnQQLREILDELQARKLKLESQVDLLQAqsqqlqkhfSLEAEAQKKQH 1553
Cdd:COG1579 89 KEYeALQKEIESLKRRIsdLEDEILELMERI---EELEEELAELEAELAELEAELEEKKA---------ELDEELAELEA 156
|
170 180 190
....*....|....*....|....*....|..
gi 2462523754 1554 LLREVTVEENNASPHFEPDL--HIEDLRKSLG 1583
Cdd:COG1579 157 ELEELEAEREELAAKIPPELlaLYERIRKRKN 188
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1236-1322 |
1.06e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.42 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1236 EQLKEEIEASEKSEQAALNAaKEKALQQLREQLEGERkeavATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQK 1315
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEK-LEKELQKLKEKLQKDA----ATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
....*..
gi 2462523754 1316 EEAQLQK 1322
Cdd:smart00935 92 ELQKILD 98
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1341-1499 |
1.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1341 YEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEllghLTGELERLQRAHEreletVRQEQH 1420
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREE----LQREEERLVQKEE-----QLDARA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1421 KRLEDLRRRHREQERKLQDLELDLETRAKDVKARlaLLEVQEETARREKQQLLDvQRQVALKSEEATATHQQLEEAQKE 1499
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNE--LYRVAGLTPEQARKLLLK-LLDAELEEEKAQRVKKIEEEADLE 173
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1064-1374 |
1.26e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1064 PEWKEAEELGEDSAASLSLQLSLQRRSTEPVAPPEQLSEAALKAMeeavaQVLEQDQRHLLESKQEKMQQLREKLCQEEE 1143
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-----TIMERFQMELKDVERKIAQQAAKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1144 EEILRLHQQKEQSLSSLR------ERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASLQKLREEL- 1216
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDtvvskiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLi 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1217 -ESQQKAERASLEQKNRQMLEQLKEEI----EASEKSEQAALNAAKEKALQQL--REQLEGERKEAVATLEKEHSAELER 1289
Cdd:TIGR00606 902 rEIKDAKEQDSPLETFLEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIHgyMKDIENKIQDGKDDYLKQKETELNT 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1290 LCSSLEAKHREvvsslQKKIQEAQQKEEAQLQKclGQVEHRVHQKSYHVAGYEHELSSLLREKRQEVEGEHERRLDKMKE 1369
Cdd:TIGR00606 982 VNAQLEECEKH-----QEKINEDMRLMRQDIDT--QKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQ 1054
|
....*
gi 2462523754 1370 EHQQV 1374
Cdd:TIGR00606 1055 EHQKL 1059
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1402-1522 |
1.40e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 43.05 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1402 ERLQRAHERELETVRQEQHkrLEDLRRRHREQERKLQDLELDLETRAKDVKA-RLALLEVQEETARREKQQLLDVQRQVA 1480
Cdd:pfam07767 199 ELLQKAVEAEKKRLKEEEK--LERVLEKIAESAATAEAREEKRKTKAQRNKEkRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462523754 1481 LKSEEAtathQQLEEAQKEHTHLLQSNQQLREILDELQARKL 1522
Cdd:pfam07767 277 IAKEIA----EKEKEREEKAEARKREKRKKKKEEKKLRPRKL 314
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1190-1319 |
1.43e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.55 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1190 VQSSTQADEDQI-RAEQEASL-----QKLREELESQQKAEraSLEQKNRQMLEQLKEEIEASEKSEQaalnaakEKALQQ 1263
Cdd:PRK00290 494 ITASSGLSDEEIeRMVKDAEAnaeedKKRKELVEARNQAD--SLIYQTEKTLKELGDKVPADEKEKI-------EAAIKE 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1264 LREQLEGERKEAVatleKEHSAELErlcssleakhrEVVSSLQKKIQEAQQKEEAQ 1319
Cdd:PRK00290 565 LKEALKGEDKEAI----KAKTEELT-----------QASQKLGEAMYQQAQAAQGA 605
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
1350-1527 |
1.50e-03 |
|
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.
Pssm-ID: 312723 [Multi-domain] Cd Length: 244 Bit Score: 42.60 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 REKRQEVEgEHERRLDKMKEEHQQ-VMAKAREQYEAEERKQRAELLGHLTGELER-LQRAHERELETVRQeqhkRLEDLR 1427
Cdd:pfam09321 53 RDALSEIS-RHELWEKKAHLKHLEsLYTQARDRFEKQSSKKNQKELEEAEQEYLSsWEDVKDQEIERVQE----RLQALQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1428 RRH-----REQERKLQD---LELDLETRAKDVKARL-ALLEVQEETARREKQQLLDV-----QRQVALKSEEATATHQQL 1493
Cdd:pfam09321 128 ALYpevsvSEEETEGQEtvtPTVDLETALGRIEESYrECVRDQEDYWKEEESKEVEMsaefrEEGGKKKSEEFQEQLGSL 207
|
170 180 190
....*....|....*....|....*....|....
gi 2462523754 1494 EEAQKEHThllqsnqqlrEILDELQARKLKLESQ 1527
Cdd:pfam09321 208 ERFLKEHS----------EELEVLEKHILKHESE 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1102-1290 |
1.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVLEQdqrhlLESKQEKMQQLREKLcqeeeEEILRLHQQKEQSLSSLRERLQkaieeeearmreeesq 1181
Cdd:COG1579 23 EHRLKELPAELAELEDE-----LAALEARLEAAKTEL-----EDLEKEIKRLELEIEEVEARIK---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1182 rlswlRAQVQSSTQADEDQIRA--EQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEK---SEQAALNAA 1256
Cdd:COG1579 77 -----KYEEQLGNVRNNKEYEAlqKEIESLKRRISDLEDEILELMERIEELEEE-LAELEAELAELEAeleEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....
gi 2462523754 1257 KEKaLQQLREQLEGERKEAVATLEKEHSAELERL 1290
Cdd:COG1579 151 LAE-LEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1199-1520 |
1.58e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRAEQEASLQKLREELESQQ--------------KAERASLEQK------NRQMLEQLKEEIEASEKSEQAALNAAKE 1258
Cdd:pfam15964 359 EQLKSELERQKERLEKELASQQekraqekealrkemKKEREELGATmlalsqNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1259 KALQQ----------LREQLEG---ERKEAvatlEKEHSAELERLCSSLEAKHREV------VSSLQKKIQEAQQK---- 1315
Cdd:pfam15964 439 QLASQemdvtkvcgeMRYQLNQtkmKKDEA----EKEHREYRTKTGRQLEIKDQEIeklgleLSESKQRLEQAQQDaara 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1316 --EEAQLQKCLGQVEHRVHqksyhvagyeheLSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAEL 1393
Cdd:pfam15964 515 reECLKLTELLGESEHQLH------------LTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1394 LGHLTGelerlQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLL 1473
Cdd:pfam15964 583 YSLLTS-----QNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMK 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462523754 1474 DVQRQVALKSEeatATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1520
Cdd:pfam15964 658 QRLRQLDKHCQ---ATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1372-1522 |
1.62e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1372 QQVMAKAREQYEAEERKQR-------AELLGHLTgelERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE--- 1441
Cdd:COG2433 353 ERVEKKVPPDVDRDEVKARvirglsiEEALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaev 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1442 LDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARK 1521
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
.
gi 2462523754 1522 L 1522
Cdd:COG2433 510 L 510
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1304-1499 |
1.62e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.81 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1304 SLQKKIQEAQQK-EEAQL-QKCLGQVEHRvHQKSYH-VAGYEHELSSLLREKRQEVEgeherrldKMKEEHQQVMAKARE 1380
Cdd:pfam15619 15 ELQNELAELQSKlEELRKeNRLLKRLQKR-QEKALGkYEGTESELPQLIARHNEEVR--------VLRERLRRLQEKERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1381 QyEAEERKQRAELLgHLTGELERLQR-AHERELETvRQEQHKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLAlle 1459
Cdd:pfam15619 86 L-ERKLKEKEAELL-RLRDQLKRLEKlSEDKNLAE-REELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLA--- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462523754 1460 vqeetarREKQQLLDVQRQVALKSEEATATHQQLEEAQKE 1499
Cdd:pfam15619 160 -------AEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1259-1529 |
1.66e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.63 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1259 KALQQLREQLEGerkeaVATLEkEHSAELERLCSSLEAKHREVVSSLQKkiqeaQQKEEAQLQKCLGQVEHrvhqksyhv 1338
Cdd:pfam09728 1 KAARELMQLLNK-----LDSPE-EKLAALCKKYAELLEEMKRLQKDLKK-----LKKKQDQLQKEKDQLQS--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 agyEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMakareqyeAEERKQRAELLGHLTGELERLQrahereletvrqe 1418
Cdd:pfam09728 61 ---ELSKAILAKSKLEKLCRELQKQNKKLKEESKKLA--------KEEEEKRKELSEKFQSTLKDIQ------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1419 qhKRLEDlrrrHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKqqllDVQRQVALKSEEATATHQQLEEAQK 1498
Cdd:pfam09728 117 --DKMEE----KSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTK----ELEVQLAEAKLQQATEEEEKKAQEK 186
|
250 260 270
....*....|....*....|....*....|.
gi 2462523754 1499 EHTHLLQSNQQLREILDELQARKLKLESQVD 1529
Cdd:pfam09728 187 EVAKARELKAQVQTLSETEKELREQLNLYVE 217
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1213-1518 |
1.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1213 REELESQQKAERASLEQKNRQMLEQLKEEIEasekSEQAALNAAKekalQQLREQLEGerkeavatlEKEHSAELERLCS 1292
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELE----KKHQQLCEEK----NALQEQLQA---------ETELCAEAEEMRA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1293 SLEAKHREVVSSLQKkiQEAQQKEEAQLQKCLGQVEHRVHQksyHVAGYEHELSS--LLREKRQEVEGEHERRLDKMKEE 1370
Cdd:pfam01576 65 RLAARKQELEEILHE--LESRLEEEEERSQQLQNEKKKMQQ---HIQDLEEQLDEeeAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1371 ----HQQVMAKAREQYEAEERKqrAELLGHLTGELERLqraheRELETVRQEQHKRLEDLRRRHREQERKLQDLEldlet 1446
Cdd:pfam01576 140 illlEDQNSKLSKERKLLEERI--SEFTSNLAEEEEKA-----KSLSKLKNKHEAMISDLEERLKKEEKGRQELE----- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1447 rakdvKARLAL----LEVQEETARReKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQ 1518
Cdd:pfam01576 208 -----KAKRKLegesTDLQEQIAEL-QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ 277
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1102-1450 |
1.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1102 EAALKAMEEAVAQVleQDQRHLLESKQEKMQQLREKLCQEEEEEilrlhQQKEQSLSSLRERLQKAiEEEEARMR---EE 1178
Cdd:COG4372 34 RKALFELDKLQEEL--EQLREELEQAREELEQLEEELEQARSEL-----EQLEEELEELNEQLQAA-QAELAQAQeelES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1179 ESQRLSWLRAQVQSSTQadEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQmLEQLKEEIEASEKSEQAALNAAKE 1258
Cdd:COG4372 106 LQEEAEELQEELEELQK--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1259 KALQQLREQLEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV 1338
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 AGYEhelssLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQE 1418
Cdd:COG4372 263 LELA-----ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340 350
....*....|....*....|....*....|..
gi 2462523754 1419 QHKRLEDLRRRHREQERKLQDLELDLETRAKD 1450
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1225-1318 |
1.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1225 ASLEQKNRQmLEQLKEEIEASEKsEQAALNAAKEKALQQLREQLEGERKEAVA--TLEKEHSAELERLCSSLEAKHrEVV 1302
Cdd:COG0542 411 EELDELERR-LEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKArwEAEKELIEEIQELKEELEQRY-GKI 487
|
90
....*....|....*.
gi 2462523754 1303 SSLQKKIQEAQQKEEA 1318
Cdd:COG0542 488 PELEKELAELEEELAE 503
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1210-1315 |
1.94e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1210 QKLREELESQQKAERASLEQKNRQmLEQLKEEIEAsEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKehsaeler 1289
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE-LQKLYEELQK-DGALLEEEREEKEQELQKKEQELQQLQQKAQQELQK-------- 87
|
90 100
....*....|....*....|....*.
gi 2462523754 1290 lcssleaKHREVVSSLQKKIQEAQQK 1315
Cdd:pfam03938 88 -------KQQELLQPIQDKINKAIKE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1008-1518 |
2.11e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1008 IEDKDDSQSSQDELQSKQSKGLEErLSPPLPHEERAQspprslateeEPPQGPEGQPEWKEAEELGEdsaaslslQLSLQ 1087
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTE-LKKALEEETRSH----------EAQLQEMRQKHTQALEELTE--------QLEQA 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1088 RRSTEPVappeqlsEAALKAMEEAVAQvLEQDQRHLLESKQEkMQQLREKLCQEEEEEILRlHQQKEQSLSSLRERLQK- 1166
Cdd:pfam01576 369 KRNKANL-------EKAKQALESENAE-LQAELRTLQQAKQD-SEHKRKKLEGQLQELQAR-LSESERQRAELAEKLSKl 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1167 --------AIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRA-------------EQEASLQKLREELESQQKAER- 1224
Cdd:pfam01576 439 qselesvsSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQklnlstrlrqledERNSLQEQLEEEEEAKRNVERq 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1225 -ASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEkaLQQLREQLEgERKEAVATLEKEHS---AELERLCSSLEaKHRE 1300
Cdd:pfam01576 519 lSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE--LEALTQQLE-EKAAAYDKLEKTKNrlqQELDDLLVDLD-HQRQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1301 VVSSLQKKiqeaqQKeeaQLQKCLGQvehrvhqksyhvagyEHELSSLLREKRQEVEG---EHERRLDKMKEEHQQvMAK 1377
Cdd:pfam01576 595 LVSNLEKK-----QK---KFDQMLAE---------------EKAISARYAEERDRAEAearEKETRALSLARALEE-ALE 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1378 AREQYEAEERKQRAEL---------LGHLTGELERLQRAHERELETVRqEQHKRLED---------LRRRHREQ------ 1433
Cdd:pfam01576 651 AKEELERTNKQLRAEMedlvsskddVGKNVHELERSKRALEQQVEEMK-TQLEELEDelqatedakLRLEVNMQalkaqf 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1434 ERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATAthqQLEEAQKEHTHLLQSNQQLREI 1513
Cdd:pfam01576 730 ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA---QIDAANKGREEAVKQLKKLQAQ 806
|
....*
gi 2462523754 1514 LDELQ 1518
Cdd:pfam01576 807 MKDLQ 811
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
1200-1359 |
2.19e-03 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 41.20 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1200 QIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATL 1279
Cdd:pfam08703 2 QVRELKERLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1280 EK--EHSAELERLCSSLEAKH-REVVSS---LQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHV-AGYEHELSSLLREK 1352
Cdd:pfam08703 82 KKrtSDKAAQERLKKEINNSHiQEVVQSikqLEEKQKRRQEKLEEKQAECLQQIKEEEPQLQAELnAEYEEKLKGLPAEV 161
|
....*..
gi 2462523754 1353 RQEVEGE 1359
Cdd:pfam08703 162 RESVKSC 168
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
1410-1483 |
2.21e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 43.01 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1410 RELETVRQEQHK---RLEDLRRRHREQERKLQD----LELDLETRAKDVKARLALL-EVQEETARREKQQLLDVQRQVAL 1481
Cdd:PRK11091 78 EQLEESRQRLSRlvaKLEEMRERDLELNVQLKDniaqLNQEIAEREKAEEARQEAFeQLKNEIKEREETQIELEQQSSLL 157
|
..
gi 2462523754 1482 KS 1483
Cdd:PRK11091 158 RS 159
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1345-1518 |
2.21e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1345 LSSLLREKRQEvEGEHERRLDKMKEEhqqvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVR--QEQHKR 1422
Cdd:pfam05557 11 LSQLQNEKKQM-ELEHKRARIELEKK-----ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1423 LEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTH 1502
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170
....*....|....*.
gi 2462523754 1503 LLQSNQQLREILDELQ 1518
Cdd:pfam05557 165 LAEAEQRIKELEFEIQ 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1430 |
2.22e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1255 AAKEKALQQLREQLeGERKEAVATLEKEHsAELERLCSSLEAKHREV---VSSLQKKIQEAQQKEEaQLQKCLGQVehrv 1331
Cdd:COG1579 13 QELDSELDRLEHRL-KELPAELAELEDEL-AALEARLEAAKTELEDLekeIKRLELEIEEVEARIK-KYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1332 hQKSYHVAGYEHELSSLlrEKRQEVEGEHERRLDKMKEEHQQVMAKAREQYE------AEERKQRAELLGHLTGELERLQ 1405
Cdd:COG1579 86 -RNNKEYEALQKEIESL--KRRISDLEDEILELMERIEELEEELAELEAELAeleaelEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*
gi 2462523754 1406 RAHERELETVRQEQHKRLEDLRRRH 1430
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRKRK 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1401-1564 |
2.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1401 LERLQRAHERELETVRQEQHKRLEDLRRRHREQERKLQDLE-----LDLETRAKDVKARLALLEVQEETARRE------- 1468
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEAKLLLQQLSELESQLAEARAElaeaear 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1469 ---------------------------KQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQS-NQQLREILDELQAR 1520
Cdd:COG3206 242 laalraqlgsgpdalpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462523754 1521 KLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQH-LLREVTVEENN 1564
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRrLEREVEVAREL 366
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1202-1529 |
2.50e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1202 RAEQEASLQKL--REELESQQKAERASLEQ---------KNRQMLEQLKEEIEASE---KSEQAALNAAKEKALQQLREQ 1267
Cdd:PRK11281 38 EADVQAQLDALnkQKLLEAEDKLVQQDLEQtlalldkidRQKEETEQLKQQLAQAPaklRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1268 LEgerKEAVATLEK---EHSAELERLCSSLEAKHREVVSS------LQKKIQEAQQkeeaQLQkclgqvehrvhqksyhv 1338
Cdd:PRK11281 118 LS---TLSLRQLESrlaQTLDQLQNAQNDLAEYNSQLVSLqtqperAQAALYANSQ----RLQ----------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1339 agyehELSSLLreKRQEVEGEHERRLDKMKEEHQQVMAKAREQYeaeerkQRAELLGH--LTgELERLQraheRELETVR 1416
Cdd:PRK11281 174 -----QIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQNDL------QRKSLEGNtqLQ-DLLQKQ----RDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1417 QEQhkrledlrrrhreQERKLQDL-ELDLETRAKDVKARLALLEVQEETARREKQQLldvqrqVALKSEEATATHQQLEE 1495
Cdd:PRK11281 236 IQR-------------LEHQLQLLqEAINSKRLTLSEKTVQEAQSQDEAARIQANPL------VAQELEINLQLSQRLLK 296
|
330 340 350
....*....|....*....|....*....|....
gi 2462523754 1496 AQKEHTHLLQSNQQLREILDELQARKLKLESQVD 1529
Cdd:PRK11281 297 ATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1067-1301 |
2.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1067 KEAEELgEDSAASLSLQLSLQRRSTEPVAPPEQLSEaalKAMEEAVAQVLE-QDQRHLLESKQEKMQQLREKLcqeeeEE 1145
Cdd:TIGR02169 798 AELSKL-EEEVSRIEARLREIEQKLNRLTLEKEYLE---KEIQELQEQRIDlKEQIKSIEKEIENLNGKKEEL-----EE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1146 ILRLHQQKEQSLSSLRERLQKAIEEEEARMREEEsQRLSWLRAQVQsstqaDEDQIRAEQEASLQKLREELESQQKAERA 1225
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELE-RKIEELEAQIE-----KKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1226 SLEQKNRQM-LEQLKEEIEASEKsEQAALNAAKEKALQQLREQLE--GERKEAVATLEKEHSAELERLcSSLEAKHREV 1301
Cdd:TIGR02169 943 DEEIPEEELsLEDVQAELQRVEE-EIRALEPVNMLAIQEYEEVLKrlDELKEKRAKLEEERKAILERI-EEYEKKKREV 1019
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1199-1267 |
2.99e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 2.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1199 DQIRAEQEASLQKLREELESQ-QKAERASLEQKNrQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1267
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIiEEARKEAEKIKE-EILAEAKEEAERILEQAKAEIEQEKEKALAELRKE 118
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1191-1418 |
2.99e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 42.51 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1191 QSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE------EIEASEKSEQAALN---AAKEKAl 1261
Cdd:pfam15450 213 ESTRLKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGldaavvQLTKFVRQNQVSLNrvlLAEQKA- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1262 QQLREQLEGERKEAVATLEKEhsaELERLCSSLEAKHREVVSSLQKKIQEAQQKEE--AQLQKCLGQVEHRVHQKSYHVA 1339
Cdd:pfam15450 292 RDAKGQLEESQAGELASYVQE---NLEAVQLAGELAQQETQGALELLQEKSQVLEGsvAELVRQVKDLSDHFLALSWRLD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1340 GYEHELSSLLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRA------ELLGHLTGELERLQ---RAHER 1410
Cdd:pfam15450 369 LQEQTLGLKLSEAKKEWEGAERKSLEDLAQWQKEVAAHLREVQEKVDSLPRQieavsdKCVLHKSDSDLKISaegKAREF 448
|
....*...
gi 2462523754 1411 ELETVRQE 1418
Cdd:pfam15450 449 EVEAMRQE 456
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1256-1525 |
3.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1256 AKEKALQQLREQLEGERKEAvatleKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEaQLQKCLGQV-EHRVHQK 1334
Cdd:COG1340 8 SSLEELEEKIEELREEIEEL-----KEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-KRDELNEKVkELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1335 syhvagyehELSSLLREKRQEVEgEHERRLDKMKEEHQQVmAKAREQYEAEERKQraellghltgELERLQRAHERELET 1414
Cdd:COG1340 82 ---------ELNEKLNELREELD-ELRKELAELNKAGGSI-DKLRKEIERLEWRQ----------QTEVLSPEEEKELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1415 VRQEQHKRLEDLRRRHrEQERKLQdlELDLETRAKDVKARLALLEVQE--ETARREKQQLLDVQRQVALKSEEATATHQQ 1492
Cdd:COG1340 141 KIKELEKELEKAKKAL-EKNEKLK--ELRAELKELRKEAEEIHKKIKElaEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462523754 1493 LEEAQKE----HTHLLQSNQQLREILDELQARKLKLE 1525
Cdd:COG1340 218 IVEAQEKadelHEEIIELQKELRELRKELKKLRKKQR 254
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1346-1466 |
3.06e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1346 SSLLREKRQEVEgeherRLDKMKEEHQQvmAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQE-QHKRLE 1424
Cdd:PRK11448 141 ENLLHALQQEVL-----TLKQQLELQAR--EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKaAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462523754 1425 DLRRRHREQERKLQDLELD-LETRAK-DVKARLALLEVQEETAR 1466
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSeEETRILiDQQLRKAGWEADSKTLR 257
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1135-1707 |
3.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1135 REKLCQEEEEEILRLHQQKEQSLSSLRERLQKaieeeearmreeesqrlswlRAQVQSSTQADEDQIRAEQeaslqklre 1214
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKK--------------------HQQLCEEKNALQEQLQAET--------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1215 ELESQQKAERASLEQKnRQMLEQLKEEIEA--SEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHsaeLERLcs 1292
Cdd:pfam01576 54 ELCAEAEEMRARLAAR-KQELEEILHELESrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ---LEKV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1293 SLEAKhrevvsslQKKIQEAQQKEEAQ---LQKCLGQVEHRVHQKSYHVAGYEHELSSL--LREKRQEVEGEHERRLDKm 1367
Cdd:pfam01576 128 TTEAK--------IKKLEEDILLLEDQnskLSKERKLLEERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKK- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1368 KEEHQQVMAKAREQYEAEE----------RKQRAELLGHLTGELERLQRAHER-ELETVRQEQhkrledLRRRHREQERK 1436
Cdd:pfam01576 199 EEKGRQELEKAKRKLEGEStdlqeqiaelQAQIAELRAQLAKKEEELQAALARlEEETAQKNN------ALKKIRELEAQ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1437 LQDLELDLET----RAKDVKARLALLE-----------------VQEETARREKQQLLDVQRQValkSEEATATHQQLEE 1495
Cdd:pfam01576 273 ISELQEDLESeraaRNKAEKQRRDLGEelealkteledtldttaAQQELRSKREQEVTELKKAL---EEETRSHEAQLQE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1496 AQKEHThllQSNQQLREILDELQARKLKLEsqvdllqaqsqqLQKHfSLEAEAQKKQHLLREVT---VEENNASPHFEPD 1572
Cdd:pfam01576 350 MRQKHT---QALEELTEQLEQAKRNKANLE------------KAKQ-ALESENAELQAELRTLQqakQDSEHKRKKLEGQ 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1573 LHIEDLRKSLGTNQTKEVSSSLsqSKEDLYLDSLSShnvwHLLSAEGVALRSAK-------------EFLVQQTR----- 1634
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKL--SKLQSELESVSS----LLNEAEGKNIKLSKdvsslesqlqdtqELLQEETRqklnl 487
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1635 SMRRRQTALKAA--QQHWRHELASAQEVAKDPPGIKA-LEDMRKNLEKETRHLDEMKSAMRKghnlLKKKEEKLNQ 1707
Cdd:pfam01576 488 STRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAqLSDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQ 559
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1401-1520 |
3.58e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1401 LERLQRAHERELETVRQEqhkrLEDLRRRHREQERKLQDLELDLETRAKdvKARLALLEVQEETARREKQQLLDVQRQVA 1480
Cdd:pfam04012 27 LEQAIRDMQSELVKARQA----LAQTIARQKQLERRLEQQTEQAKKLEE--KAQAALTKGNEELAREALAEKKSLEKQAE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462523754 1481 LKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQAR 1520
Cdd:pfam04012 101 ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR 140
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1180-1504 |
3.67e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1180 SQRLSWLRAQVQSSTQAdedQIRAEQEASLQKLREEL-ESQQKAE-------------RASLEQKNRQMLEQLKEEIEAS 1245
Cdd:NF041483 103 TQRILQEHAEHQARLQA---ELHTEAVQRRQQLDQELaERRQTVEshvnenvawaeqlRARTESQARRLLDESRAEAEQA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1246 EKSEQAALNAAKEKALQQLREQLEGERKEAVATLEK-----------------EHSAELERLCSSL-----EAKHR--EV 1301
Cdd:NF041483 180 LAAARAEAERLAEEARQRLGSEAESARAEAEAILRRarkdaerllnaastqaqEATDHAEQLRSSTaaesdQARRQaaEL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1302 VSSLQKKIQEAQQK---EEAQLQKCLGQVEHRVHQKsyhVAGYEHELSSLLREKRQEVE---GEHERRLDKMKEEHQQVM 1375
Cdd:NF041483 260 SRAAEQRMQEAEEAlreARAEAEKVVAEAKEAAAKQ---LASAESANEQRTRTAKEEIArlvGEATKEAEALKAEAEQAL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1376 AKAREQYE-----AEERKQRA-----------------ELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQ 1433
Cdd:NF041483 337 ADARAEAEklvaeAAEKARTVaaedtaaqlakaartaeEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523754 1434 ERKLQDLELD--LETRAKDVkarlallEVQEEtARR---EKQQLLD--VQRQVALKSEEATATHQQLEEAQKEHTHLL 1504
Cdd:NF041483 417 AEQLKGAAKDdtKEYRAKTV-------ELQEE-ARRlrgEAEQLRAeaVAEGERIRGEARREAVQQIEEAARTAEELL 486
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
1190-1327 |
3.78e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 40.37 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1190 VQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSE--QAALNAAKEkALQQLREQ 1267
Cdd:PRK02292 10 IRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQELSSAKLEakRERLNARKE-VLEDVRNQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523754 1268 LEgerkEAVATLEKEHSAELER-LCSSLEAKHREVVSS------LQKKIQEAQQKEEAQLQKCLGQV 1327
Cdd:PRK02292 89 VE----DEIASLDGDKREELTKsLLDAADADGVRVYSRkddedlVKSLLSDYDGLEYAGNIDCLGGV 151
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
900-1322 |
3.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 900 EPAKASEKEAPEDTVDAGEEGSRREEAAK-EPKKKASALEEGSS-DASQELEISEHMKEPQLSDSIASDPKSFHGLDFgf 977
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEkKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM-- 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 978 rsrisehlldvdvlspvlggACRQAQQPLGIEDKDDSQSSQDELQSKQSKGLEERlspplpHEERAQSPPRSLATEEEPP 1057
Cdd:PTZ00121 1579 --------------------ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK------KAEEAKIKAEELKKAEEEK 1632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1058 QGPEgQPEWKEAEElgedsaaslslqlslqRRSTEPVAPPEQlsEAALKAMEEAVAQvlEQDQRHLLESKQEKMQQlrek 1137
Cdd:PTZ00121 1633 KKVE-QLKKKEAEE----------------KKKAEELKKAEE--ENKIKAAEEAKKA--EEDKKKAEEAKKAEEDE---- 1687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1138 lcqeeeeeilrlhQQKEQSLSSLRERLQKAIEEEEARMREEesqrlswlRAQVQSSTQADEDQIRAEQEAslqklREELE 1217
Cdd:PTZ00121 1688 -------------KKAAEALKKEAEEAKKAEELKKKEAEEK--------KKAEELKKAEEENKIKAEEAK-----KEAEE 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1218 SQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQ--LREQLEGERK--------EAVATLEKEHSAEL 1287
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEedEKRRMEVDKKikdifdnfANIIEGGKEGNLVI 1821
|
410 420 430
....*....|....*....|....*....|....*
gi 2462523754 1288 ERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQK 1322
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNK 1856
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1197-1281 |
4.24e-03 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.31 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1197 DEDQiRAEQEASLQKLREELESQQKA-ERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAK----EKALQQLREQLEGE 1271
Cdd:pfam12729 73 DPAE-RDELLKDIEELRAEIDKLLEKyEKTILTDEEKKLFAEFKENLNAYRAVRNKVLELAKagnkDEAYQLYKTEGRPA 151
|
90
....*....|
gi 2462523754 1272 RKEAVATLEK 1281
Cdd:pfam12729 152 REAMIEALEE 161
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1195-1321 |
4.53e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1195 QADEDQIRAEQeASLQKLREELesQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEkALQQLREQLEGERKE 1274
Cdd:pfam00529 57 QAALDSAEAQL-AKAQAQVARL--QAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA-QLAQAQIDLARRRVL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462523754 1275 AVATL-EKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQ 1321
Cdd:pfam00529 133 APIGGiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA 180
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1082-1509 |
4.60e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1082 LQLSLQRRSTEPVAPPEQLSEAALKAMEEAVAQVlEQDQRHLLESKQEKMQQLrEKLCQEEEEEILRLHQQKEQSLSSLR 1161
Cdd:pfam07111 94 MRLEAQAMELDALAVAEKAGQAEAEGLRAALAGA-EMVRKNLEEGSQRELEEI-QRLHQEQLSSLTQAHEEALSSLTSKA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1162 ERLQKAIEEEEARMREEESQRLSWLRAQVQSSTQADEDQIRAEQEASL-QKLREELESQQKAE--RASLEQKNRQMLEQL 1238
Cdd:pfam07111 172 EGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLvESLRKYVGEQVPPEvhSQTWELERQELLDTM 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1239 KeEIEASEKSEQAALNAAKEKaLQQLREQLEGERKEAVATLEKEHSAELE--RLCSSLEAKHREVVSSL--QKKIQEAQQ 1314
Cdd:pfam07111 252 Q-HLQEDRADLQATVELLQVR-VQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWREKVFALmvQLKAQDLEH 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1315 KEE-AQLQKCLGQVEHRVHQKSYHVAgyehELSSLLREKRQEVEGEH-ERRLDKMKEEHQQVMAKAREQYEAEERKQRAE 1392
Cdd:pfam07111 330 RDSvKQLRGQVAELQEQVTSQSQEQA----ILQRALQDKAAEVEVERmSAKGLQMELSRAQEARRRQQQQTASAEEQLKF 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1393 LLGHLTGELERLQRAHERELETVRQ--EQHKRLE-DLRRRHREQ---ERKLQDLELDLETRAK-------DVKARLALLE 1459
Cdd:pfam07111 406 VVNAMSSTQIWLETTMTRVEQAVARipSLSNRLSyAVRKVHTIKglmARKVALAQLRQESCPPpppappvDADLSLELEQ 485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1460 VQEETARREKQQLLD---VQRQVALKSEEATATHQQLEEAQKEHTHLLQSNQQ 1509
Cdd:pfam07111 486 LREERNRLDAELQLSahlIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQE 538
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1086-1276 |
4.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1086 LQRRSTEPVAPPEQLSEA--ALKAMEEAVAQVLEQDQRHLLESKQEKMQQLREKLCQEEEEEILRLHQQKEQsLSSLRER 1163
Cdd:COG4717 325 LAALGLPPDLSPEELLELldRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1164 LQKAieeeearmreeESQRLSWLRAQVQSSTQADEDQIRAE---QEASLQKLREELESQQKaERASLEQKNRQM-----L 1235
Cdd:COG4717 404 LEEL-----------EEQLEELLGELEELLEALDEEELEEEleeLEEELEELEEELEELRE-ELAELEAELEQLeedgeL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462523754 1236 EQLKEEIE-----ASEKSEQAALNAAKEKALQQLREQLEGERKEAV 1276
Cdd:COG4717 472 AELLQELEelkaeLRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1342-1473 |
4.88e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.65 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1342 EHELSSLLREKRQEVEGEHERRLDKMKEE-HQQVMAKAREQYEAEERKQRAEllghltgelERLQRAHERELETVRQEQH 1420
Cdd:pfam15346 21 AKRVEEELEKRKDEIEAEVERRVEEARKImEKQVLEELEREREAELEEERRK---------EEEERKKREELERILEENN 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1421 KRLEDLRRRHREQERKlqdlELDLETRAKDVKARLAllEVQEETARREKQQLL 1473
Cdd:pfam15346 92 RKIEEAQRKEAEERLA----MLEEQRRMKEERQRRE--KEEEEREKREQQKIL 138
|
|
| PRK13895 |
PRK13895 |
conjugal transfer protein TraM; Provisional |
1229-1299 |
4.92e-03 |
|
conjugal transfer protein TraM; Provisional
Pssm-ID: 184378 Cd Length: 144 Bit Score: 39.27 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1229 QKNRQ-MLEQLKEEIE---------ASEKSEQ---AALNAAKEKALQQLREQLegerKEAVATLEKEHSAELERLCSSLE 1295
Cdd:PRK13895 41 AKAQQeMLDQFKEELEsiasrwgddAKEKAERilnAALAASKEAMAKGMQEGA----KAAAEAVRREISASLAELAAPVR 116
|
....
gi 2462523754 1296 AKHR 1299
Cdd:PRK13895 117 EARR 120
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1184-1283 |
5.36e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1184 SWLRAQVQSSTQADEDQIRAE---QEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKA 1260
Cdd:smart00935 13 SPAGKAAQKQLEKEFKKRQAElekLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEE 92
|
90 100
....*....|....*....|...
gi 2462523754 1261 LQQLREQLegerKEAVATLEKEH 1283
Cdd:smart00935 93 LQKILDKI----NKAIKEVAKKK 111
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1261-1455 |
5.77e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1261 LQQLREQLEGERKEAVATLEKEhsaeLERLCSSLEAKHREVVSSLQKKIQEAQQKeeaqlqkcLGQvehrvhqksyHVAG 1340
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKE----TEALRERLQKDLEEVRAKLEPYLEELQAK--------LGQ----------NVEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1341 YEHELSSLLREKRQEVEgeheRRLDKMKEEHQQVMAKAREQYEAEERKQRAellgHLTGELERLQRAHERELETVRQEQH 1420
Cdd:pfam01442 71 LRQRLEPYTEELRKRLN----ADAEELQEKLAPYGEELRERLEQNVDALRA----RLAPYAEELRQKLAERLEELKESLA 142
|
170 180 190
....*....|....*....|....*....|....*
gi 2462523754 1421 KRLEDLRRRHREQerkLQDLELDLETRAKDVKARL 1455
Cdd:pfam01442 143 PYAEEVQAQLSQR---LQELREKLEPQAEDLREKL 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1362-1505 |
5.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1362 RRLDKMKEEHQQVMAKAREqyeaEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHREQER---KLQ 1438
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQK----EAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462523754 1439 DLELDLETRAKDVKARLALLEVQEETARREKQQLL----DVQRQVALKSEEATATHQ--QLEEAQKEHTHLLQ 1505
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAgltpEQARKLLLKLLDAELEEEkaQRVKKIEEEADLEA 174
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
1186-1332 |
6.04e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 41.11 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1186 LRAQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQM-LEQLKEEIEASEKseqaaLNAAKEKALQQL 1264
Cdd:pfam17060 106 LKEDVKSSPRSEADSLGTPIKVDLLRNLKPQESPETPRRINRKYKSLELrVESMKDELEFKDE-----TIMEKDRELTEL 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523754 1265 REQLeGERKEAVATLEKEHS-----AELERLCSSLEA-KHREVVSSLQKKIQEaQQKEEAQLQKCLGQVEHRVH 1332
Cdd:pfam17060 181 TSTI-SKLKDKYDFLSREFEfykqhHEHGGNNSIKTAtKHEFIISELKRKLQE-QNRLIRILQEQIQFDPGALH 252
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1186-1269 |
6.44e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 39.55 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1186 LRAQVQSSTQADEDQIRAEQEAslQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQA---------ALNAA 1256
Cdd:PRK07352 66 LRQAAQALAEAQQKLAQAQQEA--ERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQErviaqlrreAAELA 143
|
90
....*....|...
gi 2462523754 1257 KEKALQQLREQLE 1269
Cdd:PRK07352 144 IAKAESQLPGRLD 156
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1191-1392 |
6.59e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1191 QSSTQADEDQIRAEQ-EASLQKLREELEsQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAALNAAkeKALQQLREQLE 1269
Cdd:pfam05701 388 QAAQEAEEAKSLAQAaREELRKAKEEAE-QAKAAASTVESR----LEAVLKEIEAAKASEKLALAAI--KALQESESSAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1270 GERKEAVA---TLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQqkeeaqlqkclgqvehrvhqksyhvagyEHELS 1346
Cdd:pfam05701 461 STNQEDSPrgvTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAK----------------------------ESELR 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462523754 1347 SLlrEKRQEVEGEHERRLDKMKEEHQQVmAKARE---QYEAEERKQRAE 1392
Cdd:pfam05701 513 SL--EKLEEVNREMEERKEALKIALEKA-EKAKEgklAAEQELRKWRAE 558
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1206-1520 |
6.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1206 EASLQKLREELESQQkaerasLEQKNRQMLEQLKEEI-------------EASEKSEQAAlnaAKEKALQQLREQLEGER 1272
Cdd:PRK04863 236 EAALRENRMTLEAIR------VTQSDRDLFKHLITEStnyvaadymrhanERRVHLEEAL---ELRRELYTSRRQLAAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1273 KEAVATLEKEhsAELERLCSSLEAKHREVVSSLQKkIQEAQQKEEaQLQKCLGQVEhrvhqksyhvagyehelssllrek 1352
Cdd:PRK04863 307 YRLVEMAREL--AELNEAESDLEQDYQAASDHLNL-VQTALRQQE-KIERYQADLE------------------------ 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1353 rqevegEHERRLdkmkEEHQQVMAKAREQY-EAEERKQRAEL-LGHLTGELERLQRAHEreletvrqEQHKRLEDLR--- 1427
Cdd:PRK04863 359 ------ELEERL----EEQNEVVEEADEQQeENEARAEAAEEeVDELKSQLADYQQALD--------VQQTRAIQYQqav 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1428 RRHREQERKLQDLELDLEtrakDVKARLALLEVQEETA---RREKQQLLDV------QRQVALKS----------EEATA 1488
Cdd:PRK04863 421 QALERAKQLCGLPDLTAD----NAEDWLEEFQAKEQEAteeLLSLEQKLSVaqaahsQFEQAYQLvrkiagevsrSEAWD 496
|
330 340 350
....*....|....*....|....*....|..
gi 2462523754 1489 THQQLEEAQKEHTHLLQSNQQLREILDELQAR 1520
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQR 528
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1371-1504 |
7.13e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 38.70 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1371 HQQVMAKAREQYEAEerkqRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLRRRHR-EQERKLQDLELDLETRAK 1449
Cdd:pfam12474 1 HQLQKEQQKDRFEQE----RQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1450 DVKA---RLALLEVQEET-ARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLL 1504
Cdd:pfam12474 77 ELKQeveKLPKFQRKEAKrQRKEELELEQKHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1205-1488 |
7.32e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 41.36 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1205 QEASLQKLREELE-----SQQKAERASLEQKNRQMLEQL-KEEIEASEKSEQAALNAAkEKALQQLREQL-EGERKEAVA 1277
Cdd:pfam15450 40 EHATLSLLRELLQvrahvQLQDSELKQLRQEVQQAARAPeKEALEFPGPQNQNQMQAL-DKRLVEVREALtQIRRKQALQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1278 TLEKEHSAE-----LERLCSSL--EAKHREVV-SSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLL 1349
Cdd:pfam15450 119 DSERKGAEQeanlrLTKLTGKLkqEEQGREAAcSALQKSQEEASQKVDHEVARMQAQVTKLGEEMSLRFLKREAKLCSFL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1350 R------EKRQEVEG----EHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQ 1419
Cdd:pfam15450 199 QksflalEKRMKASEstrlKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLDAAVVQLTKFVRQNQ 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462523754 1420 HKRLEDLRRRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATA 1488
Cdd:pfam15450 279 VSLNRVLLAEQKARDAKGQLEESQAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVA 347
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1227-1422 |
7.32e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.54 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1227 LEQKNRQMLEQ-LKEEIEASEKSEQAALNAAKEKALQQLREQLEGERKEAVATLEKEHSAELErlcssLEAKHREVVSSL 1305
Cdd:PTZ00491 641 VDERTRDSLQKsVQLAIEITTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1306 QKKiQEAQQKEEAQLQKClgqvehrvhQKSYHVAGyehelsslLREKRQEVEGEHErrLDKMKEEHQQvmakareqyEAE 1385
Cdd:PTZ00491 716 QSR-AEALAEAEARLIEA---------EAEVEQAE--------LRAKALRIEAEAE--LEKLRKRQEL---------ELE 766
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462523754 1386 ERKQRAELlghltgELERlqrahERELETVRQEQHKR 1422
Cdd:PTZ00491 767 YEQAQNEL------EIAK-----AKELADIEATKFER 792
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1087-1528 |
7.44e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1087 QRRSTEPVAPPEQLSEA---------ALKAMEEAVAQVLEQDQR--------HLLESKQEKMQQLREKLC--QEEEEEIL 1147
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKfdeifsatrYIKALETLRQVRQTQGQKvqehqmelKYLKQYKEKACEIRDQITskEAQLESSR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1148 RLHQQKEQSLSSLRERLQ----------------KAIEEEEARMREEESQrLSWLRAQVQSSTQADEDQI-RAEQEASLQ 1210
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKeiehnlskimkldneiKALKSRKKQMEKDNSE-LELKMEKVFQGTDEQLNDLyHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1211 KLREELESQQKAERASleqKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQ--------QLREQLEGERKEAVATLEKE 1282
Cdd:TIGR00606 317 KERELVDCQRELEKLN---KERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsliqslATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1283 HSAELERLCSSLEAKH-REVVSSLQKKIQEAqQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSSLLREKrQEVEGEHE 1361
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTaAQLCADLQSKERLK-QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1362 RRLDKMKE--EHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKrledlrrrhREQERKLQD 1439
Cdd:TIGR00606 472 RILELDQElrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT---------RTQMEMLTK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1440 LELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQvalKSEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQA 1519
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS---KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
....*....
gi 2462523754 1520 RKLKLESQV 1528
Cdd:TIGR00606 620 QLSSYEDKL 628
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1193-1326 |
7.51e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.16 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1193 STQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKE--EIEASEKSEQAALNAAK------EKALQQL 1264
Cdd:PTZ00491 660 TTKSQEAAARHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAEsaAVESSGQSRAEALAEAEarlieaEAEVEQA 739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523754 1265 REQLEGERKEAVATLEKEHsAELErlcssLEAKHREVVSSL----QKKIQEAQQKEEAQLQKCLGQ 1326
Cdd:PTZ00491 740 ELRAKALRIEAEAELEKLR-KRQE-----LELEYEQAQNELeiakAKELADIEATKFERIVEALGR 799
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1214-1394 |
7.59e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1214 EELESQQKaeraSLEQKNRQmLEQLKEEIEAsekseqaalnaaKEKALQQLREQLEGERKEAVATLEKEhsaelerlcss 1293
Cdd:PRK00409 523 ASLEELER----ELEQKAEE-AEALLKEAEK------------LKEELEEKKEKLQEEEDKLLEEAEKE----------- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1294 leakhrevvssLQKKIQEAqQKEEAQLQKCLgqvehRVHQKSYHVAGYEHELSsllrEKRQEVEGEHErrldkMKEEHQQ 1373
Cdd:PRK00409 575 -----------AQQAIKEA-KKEADEIIKEL-----RQLQKGGYASVKAHELI----EARKRLNKANE-----KKEKKKK 628
|
170 180
....*....|....*....|....*..
gi 2462523754 1374 VMAKAREQYEAEER------KQRAELL 1394
Cdd:PRK00409 629 KQKEKQEELKVGDEvkylslGQKGEVL 655
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1197-1281 |
7.70e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1197 DEDQIRAEQEasLQKLREELESQQKAERASLEQKnrqmLEQLKEEIEASEKSEQAA------LNAAKeKALQQLREQLEg 1270
Cdd:cd22656 171 DEGGAIARKE--IKDLQKELEKLNEEYAAKLKAK----IDELKALIADDEAKLAAAlrliadLTAAD-TDLDNLLALIG- 242
|
90
....*....|.
gi 2462523754 1271 erkEAVATLEK 1281
Cdd:cd22656 243 ---PAIPALEK 250
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1188-1562 |
8.30e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 41.33 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1188 AQVQSSTQADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQ 1267
Cdd:COG2203 338 DQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1268 LEGERKEAVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQEAQQKEEAQLQKCLGQVEHRVHQKSYHVAGYEHELSS 1347
Cdd:COG2203 418 LEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLAL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1348 LLREKRQEVEGEHERRLDKMKEEHQQVMAKAREQYEAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEDLR 1427
Cdd:COG2203 498 LALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLI 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1428 RRHREQERKLQDLELDLETRAKDVKARLALLEVQEETARREKQQLLDVQRQVALKSEEATATHQQLEEAQKEHTHLLQSN 1507
Cdd:COG2203 578 ELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLR 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462523754 1508 QQLREILDELQARKLKLESQVDLLQAQSQQLQKHFSLEAEAQKKQHLLREVTVEE 1562
Cdd:COG2203 658 ALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLEV 712
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1409-1527 |
8.35e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1409 ERELETVRQE------QHKRLEDLRRRHREQERKLQDleldletrakdvKARLALLEVQEETARR--EKQQLLDvqrqva 1480
Cdd:COG1842 36 EEDLVEARQAlaqviaNQKRLERQLEELEAEAEKWEE------------KARLALEKGREDLAREalERKAELE------ 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462523754 1481 lksEEATATHQQLEEAQKEHTHLLQSNQQLREILDELQARKLKLESQ 1527
Cdd:COG1842 98 ---AQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKAR 141
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1374-1528 |
8.79e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1374 VMAKAREQY--EAEERKQRAELLGHLTGELERLQRAHERELETVRQEQHKRLEdlRRRHREQERKLQDLELDLETRAKDV 1451
Cdd:PRK12705 23 VLLKKRQRLakEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRE--REELQREEERLVQKEEQLDARAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523754 1452 KARLALLEVQEETARREKQQLLDVQRQVALKSEEATAthqqleeaqkehthlLQSNQQLREILDELQArKLKLESQV 1528
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAG---------------LTPEQARKLLLKLLDA-ELEEEKAQ 161
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1195-1311 |
8.86e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1195 QADEDQIRAEQEASLQKLREELESQQKAERASLEQKNRQMLEQLKEeieasekseqaalnaAKEKALQQLREQLEGERKE 1274
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQER---------------SYEEHLRQLKEKMEEEREN 252
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462523754 1275 AVATLEKEHSAELERLCSSLEAKHREVVSSLQKKIQE 1311
Cdd:cd16269 253 LLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1196-1275 |
9.73e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523754 1196 ADEDQIRAEQEASLQKLREELESQ-----QKAERASLEQKNRQMLEQLKEEIEASEKSEQAALNAAKEKALQQLREQLEg 1270
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQarekaQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ- 216
|
....*
gi 2462523754 1271 ERKEA 1275
Cdd:PRK11448 217 KRKEI 221
|
|
| |
